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1 tivity through conformational changes at the selectivity filter.
2 helix S6 at an alanine hinge just below the selectivity filter.
3 inner pore region nearest the bottom of the selectivity filter.
4 lly be occupied by K(+) before it enters the selectivity filter.
5 t barttin binding sites, dimer interface and selectivity filter.
6 ct interdomain interface movement behind the selectivity filter.
7 the C-type inactivation gate at or near the selectivity filter.
8 into the high electric field of an inactive selectivity filter.
9 dynamics of the alpha-helical region of the selectivity filter.
10 +) by a ring of aspartate side chains in the selectivity filter.
11 of the channel act as a pH sensor and proton selectivity filter.
12 fic heavy ((13)C(18)O) isotope labels in the selectivity filter.
13 H to probe the affinity for potassium at the selectivity filter.
14 mutagenesis, these rings appear to form the selectivity filter.
15 diameter of 1.8 nm and located the channel's selectivity filter.
16 ibutable to simply a modification of the CCR selectivity filter.
17 racellular and intracellular entrance of the selectivity filter.
18 ular side of the membrane and another in the selectivity filter.
19 the channel structure and its bearing on the selectivity filter.
20 ideas about the location and function of the selectivity filter.
21 NaK2K outside the immediate vicinity of the selectivity filter.
22 llular entryway, the gate must be within the selectivity filter.
23 sequences unrelated to any other known ionic selectivity filter.
24 including the conducting conformation of the selectivity filter.
25 rus is a proton channel that uses His37 as a selectivity filter.
26 water in the central cavity adjacent to the selectivity filter.
27 lity of Ca(2+) to a site at the entry to the selectivity filter.
28 m a conformational change near the channel's selectivity filter.
29 presence of four glutamate residues in their selectivity filter.
30 llowed by ion expulsion at the extracellular selectivity filter.
31 mity to Lys-1237 of the domain III pore-loop selectivity filter.
32 R has four aspartate residues in its GGGIGDE selectivity filter.
33 n previously to increase the diameter of the selectivity filter.
34 of the pore and an inactivation gate at the selectivity filter.
35 n by buried water molecules bound behind the selectivity filter.
36 the fact that both ions can bind within the selectivity filter.
37 e chains lining the extracellular end of the selectivity filter.
38 as a wide extracellular 'mouth' with a short selectivity filter.
39 cts directly with conducting ions inside the selectivity filter.
40 s define an extracellular ion pathway to the selectivity filter.
41 site thus serve as characteristic substrate selectivity filter.
42 ffects the potassium binding affinity of the selectivity filter.
43 composition and solvent accessibility of the selectivity filter.
44 f of Ca(2+) inactivation of the channel pore selectivity filter.
45 l reflecting the mixed permeability of their selectivity filter.
46 vidently, the HG does not act as a secondary selectivity filter.
47 e hydrogen bonding network that controls the selectivity filter.
48 isoleucine and a conserved threonine in the selectivity filter.
49 n-bound configuration) of the K(+) channel's selectivity filter.
50 state but that it may not directly enter the selectivity filter.
51 probe specific ion binding sites within the selectivity filter.
52 ponds to a "constricted" conformation of the selectivity filter.
53 ar entrance and a second constriction at the selectivity filter.
54 cal marker of conformational dynamics at the selectivity filter.
55 y encoded at Y671, a residue proximal to the selectivity filter.
56 x transmembrane helices, a pore helix, and a selectivity filter.
57 s) showed radical differences in their anion selectivity filters.
58 onovalent Na(+) with H3O(+) in various model selectivity filters.
60 (+) ions permeate in single file through the selectivity filter, a narrow pore lined by backbone carb
61 they may be activated by a change within the selectivity filter, a narrow region at the extracellular
62 ion I4897T results in destabilization of the selectivity filter, a possible cause of the CCD-specific
63 ed hypothesis that multiple K(+) ions in the selectivity filter act to mutually destabilize binding.
66 tinuous alpha helix in which the Gly-Ala-Ser selectivity filter adopts an extended, belt-like conform
68 ner transmembrane helix (98-103), and in the selectivity filter, all of which resemble changes seen u
69 tors show that both compounds bind below the selectivity filter and are trapped in the vestibule by t
71 0.2 mus, with multiple cations occupying the selectivity filter and cytosolic vestibule, but not the
72 ore, optimizing K(+) ion coordination in the selectivity filter and increasing current amplitudes.
73 structural and dynamic coupling between the selectivity filter and intracellular constriction point
74 uction pore involving both the extracellular selectivity filter and intracellular helix bundle crossi
75 ve focused on ion occupancy of the channel's selectivity filter and its ability to alter gating, with
77 conformational landscape of the K(+) channel selectivity filter and its dependence on the state of th
78 ion permeation pathway is constricted at the selectivity filter and near the cytoplasmic end of S6, s
80 k in a bottle - binding in the extracellular selectivity filter and sterically occluding ion conducti
81 h the innermost acidic residue (D523) of the selectivity filter and subsequent long-term channel inac
82 one or two hydrated Ca(2+) ions bound in the selectivity filter and supports a 'knock-off' mechanism
83 structural and dynamic coupling between the selectivity filter and the channel scaffold, which has s
85 a loss of affinity for potassium ions at the selectivity filter and therefore to channel inactivation
86 us crystallographic views, we found that the selectivity filter and turret region, coupled to the sur
87 transient intermediate states that serve as selectivity filters and precede the formation of the sta
88 (i) as a channel blocker at the base of the selectivity filter, and (ii) as a modulator to restrict
90 ses a DIME sequence thought to form a Ca(2+) selectivity filter, and also regulatory EMRE, MICU1, and
91 n gate to "remember" the conformation of the selectivity filter, and hence KcsA requires a different
92 he detailed architecture of the K(+) channel selectivity filter, and not only its equilibrium ion pre
93 t with directly neighboring K(+) ions in the selectivity filter, and our model offers an intuitive ex
95 , permeation, selectivity, and gating at the selectivity filter are all governed by the thermodynamic
96 that buried water molecules bound behind the selectivity filter are at the origin of the slowness of
98 oth an inner and outer gate within the CLC-2 selectivity filter, as a function of GLUex protonation.
99 the outer pore, including the pore helix and selectivity filter, as well as pronounced dilation of a
100 t the nonmetal-ligating Lys in the DKEA/DEKA selectivity filter attenuates metal-protein interactions
101 uctures provide an unprecedented view of the selectivity filter backbone in its collapsed deep C-type
102 ate that the presence of a Ba(2+) ion in the selectivity filter boosts the specificity of K(+) bindin
103 on had little impact on Na(+) binding to the selectivity filter, but disrupted the binding of ammoniu
104 the potassium affinity at the extracellular selectivity filter by more than three orders of magnitud
105 other potassium channels, K2P channels use a selectivity filter 'C-type' gate as the principal gating
106 Unlike C-type inactivation, a consequence of selectivity filter closure, in many K(+) channels, the r
107 ough the pore is restricted by a hydrophobic selectivity filter comprising disordered phenylalanine-g
108 ransition from the inactivated nonconductive selectivity filter conformation toward the conductive co
109 l and crystallographic analyses of a calcium selectivity filter constructed in the homotetrameric bac
111 brane helix 1) and the pore helix behind the selectivity filter contributes to K(+) channel inactivat
112 nd strong evidence that the channel's proton selectivity filter controls blocker binding cooperativit
115 ion that the constricted conformation of the selectivity filter corresponds to the functional C-type
116 We further suggest that stability of the selectivity filter critically depends on the interaction
117 itro permeability measurements suggests that selectivity filter cross-sectional area predicts urea bu
118 mpetition between Mg(2+) and Ca(2+) in model selectivity filters depends on the degree of metal hydra
119 cturally different from KcsA because the NaK selectivity filter does not collapse under low-cation co
121 and substituting one or two residues in the selectivity filter drastically increased the IC(50) valu
127 at the site interacts with K(+) ions in the selectivity filter, facilitating a conformational change
128 Although V169(5.30) is considered to be a selectivity filter for A(3)R binders, when it was mutate
129 lso demonstrate that the Arg-147 is a strong selectivity filter for carboxylate-containing substrates
132 activation/deactivation and the other at the selectivity filter for slow C-type inactivation/recovery
133 f the NPC may explain how NPC functions as a selectivity filter for transport of large molecules and
134 bacterium Tsukamurella paurometabola with a selectivity filter formed by an uncommon proline-rich se
136 odifications are not believed to prevent the selectivity filter from adopting the constricted conform
138 on occupancy, and thus, conductivity, of the selectivity filter gate that is coupled to an imperfectl
139 y coupled gates, the activation gate and the selectivity filter gate, that control channel opening, c
140 d external protons control intracellular and selectivity filter gates to modulate TASK2 activity.
141 obe the structural changes that occur during selectivity filter gating in Kv11.1 channels, at near at
146 st RNA targets, and that disruptions of this selectivity filter give rise to autoimmune diseases.
148 An activation process, occurring at the selectivity filter, has been recently proposed for sever
149 ivation is modulated by ion binding near the selectivity filter; however, the molecular forces that i
150 s with an open intracellular gate revealed a selectivity filter in a constricted conformation similar
151 uctures of KcsA's mutants that stabilize the selectivity filter in its conductive (E71A, at 2.25 A) a
153 The scoop loop thereby acts as an additional selectivity filter in shaping the repertoire of presente
154 oactivation at F579AzF, a residue behind the selectivity filter in the M2 segment, had extraordinaril
155 n nonconductive and conductive states of the selectivity filter in which to test competitive binding
157 experimental data and help to elucidate the selectivity filters in the Mg(2+)-selective TRPM6 and Co
158 consistent with structural evidence that the selectivity filters in these channels are dynamic, they
160 ly induces an asymmetric conformation of the selectivity filter, in which partially dehydrated Ca(2+)
161 hus, unlike ion channels that have a single "selectivity filter," in bestrophin, distinct regions of
163 ral elements supporting the integrity of the selectivity filter; instead they play a crucial dynamic
164 gh this modification is believed to lock the selectivity filter into its conductive conformation, whe
166 odel in which the loss of K(+) ions from the selectivity filter is a major factor in promoting inacti
167 for Mg(2+) over Ca(2+) in the Mg(2+) channel selectivity filter is a pore that is sufficiently large
170 o channels with an inactivated or conductive selectivity filter is different from K(+) ion binding to
172 whether the constricted conformation of the selectivity filter is in fact the C-type inactivated sta
174 cient for Na(+) selectivity and why the DKEA selectivity filter is less Na(+)-selective than the DEKA
177 a voltage stimulus, whereas the gate at the selectivity filter is responsible for C-type inactivatio
178 long molecular dynamics simulations, how the selectivity filter is sterically locked in the inactive
179 the potassium affinity at the extracellular selectivity filter is strongly dependent on proton bindi
181 ithin the pore, the aromatic/arginine (ar/R) selectivity filter, is thought to control solute permeab
182 ically different motional and conformational selectivity filter landscape in a mutant that mimics vol
183 tion of the voltage sensor S4 helix, an open selectivity filter leading to an open activation gate at
185 dified semisynthetic KcsA channels along the selectivity filter led to the conclusion that the constr
189 ants, located in the pore turret (G618W) and selectivity filter (M644I), resulted in significantly re
192 A subtle structural feature of the hERG selectivity filter might correlate with its fast inactiv
195 onium and hydrazinium, the charge-conserving selectivity filter mutation (E191D) yielded substantial
196 tracellular pore constriction and within the selectivity filter near the extracellular side but the s
197 sible influx and efflux of Na(+) through the selectivity filter occurred spontaneously during simulat
198 nd temporal distribution of water behind the selectivity filter of a membrane-embedded K(+) channel i
201 hly conserved aromatic residue near the pore selectivity filter of claudins contributes to cation sel
202 o a Na(+)-selective channel by mimicking the selectivity filter of HsTPC2 and identified key residues
203 FABC complex with a potassium ion within the selectivity filter of KdpA and a water molecule at a can
204 iments also suggest water is proximal to the selectivity filter of KirBac1.1 in the open-activated st
206 llular K+ ions can block the entrance to the selectivity filter of Na(v)Ab in the presence of applied
209 barriers preclude Na(+) ions to permeate the selectivity filter of prokaryotic Na(+)-channels when on
211 To examine permeation of Na(+) through the selectivity filter of the channel, we performed large-sc
214 binding site in the constricted state of the selectivity filter of the KcsA channel when the intracel
216 marily binds to the innermost site S4 of the selectivity filter of the open-gate conformation and als
218 y for K(+) to study ion interaction with the selectivity filter of the prototypical full-length K(+)
220 f MitTx action, defines the structure of the selectivity filter of voltage-independent, sodium-select
221 that single amino acid substitutions in the selectivity filters of AQP1, AQP4 and AQP3 differentiall
222 the Glu from domain II/III in the EEEE/DEEA selectivity filters of Ca(2+)-selective channels to Lys
223 sis was used to introduce d-Alanine into the selectivity filters of the KcsA channel and the voltage-
224 in barttin-binding sites, dimer interface or selectivity filter often have severe functional conseque
225 eation in the absence of activators: the ion selectivity filter on the external side of the pore and
226 of the pore on the intracellular side of the selectivity filter, physically blocking the ion-conducti
230 In addition to ionic discrimination, the selectivity filter regulates the flow of ions across the
232 d and are associated with side chains of the selectivity filter residues, rather than polypeptide bac
233 d rival cations such as Na(+) depends on the selectivity filter's (1) histidine protonation state, (2
234 ammonium at the most cytoplasmic site in the selectivity filter (S4) suggests that such a site, when
235 annels, but instead possess unique pore-loop selectivity filter sequences unrelated to any other know
236 evious studies suggested that the pore helix/selectivity filter serves as the activation gate in Slo2
237 ion mutation N629D at the outer mouth of the selectivity filter (SF) disrupts inactivation and K(+)-s
240 vation at a gate inside the highly conserved selectivity filter (SF) region near the extracellular si
241 equires an aspartate near an arginine in the selectivity filter (SF), a narrow region that dictates p
242 er keys to open K(+) channels gated at their selectivity filter (SF), including many two-pore domain
243 athway, three relatively narrow regions (the selectivity filter (SF), the inner helix bundle crossing
244 ode involves a change in conformation at the selectivity filter (SF), which impedes ion flow at this
248 that the number of ion binding sites in the selectivity filter shifts the equilibrium distribution o
249 ium (DMA(+)), the side chain of Glu66 in the selectivity filter shows multiple conformations and the
250 e role of a hydrogen bond network behind the selectivity filter, side-chain conformational dynamics,
251 nnels have an intramembrane vestibule with a selectivity filter situated above and a gate with four p
252 transient period of ion conduction until the selectivity filter spontaneously undergoes a conformatio
253 hout producing discernable alteration of the selectivity filter structure and is oriented to project
256 he invariant ring of charged residues in the selectivity filter that governs calcium selectivity in c
257 and involves a conformational change in the selectivity filter that is mediated by cooperative subun
258 ated with structural changes around the K(+)-selectivity filter that may have implications for mechan
260 d Na(+) channels, which is controlled by the selectivity filter (the narrowest region of an open pore
262 while helping Na(+) ions diffuse within the selectivity filter, the conformational flexibility of E1
263 nic nonannular lipids close to the channel's selectivity filter, the influence of nonannular lipid bi
265 e of the K(+) binding sites in the channel's selectivity filter, the S4 site, also binds Ba(2+) ions,
266 m away but do not alter the structure of the selectivity filter-the commonly presumed activation gate
267 csA channel removes steric restraints at the selectivity filter, thus resulting in structural fluctua
268 substitutions in the protein backbone of the selectivity filter to alter ion binding at specific site
269 ng ion permeation, including widening of the selectivity filter to enhance calcium permeability and o
270 the stimulus closes the gate and allows the selectivity filter to interconvert back to its conductiv
271 cal similarity of the x-ray structure of the selectivity filter to other K(+) channels, the structure
273 st a unique allosteric pathway that ties the selectivity filter to the activation gate through intera
275 complex hydrogen-bond network that link the selectivity filter to the surrounding pore helices diffe
276 +, three Na+ ions move favorably through the selectivity filter together as a unit in a loose "knock-
277 ammalian voltage-gated calcium channel (CaV) selectivity filters, together with functional studies, s
279 are primarily occupied by K(+) ions in their selectivity filters under physiological conditions, demo
280 rplay between the intracellular gate and the selectivity filter underlies the structural basis for ga
283 volve multiple conformational changes at the selectivity filter, we propose that the BK channel's nor
284 ectivity of TRPV6 originates from the narrow selectivity filter, where Ca(2+) ions are directly coord
285 n which chemical synthesis is limited to the selectivity filter whereas the rest of the protein is ob
286 w end of the funnel serves as a broad cation selectivity filter, whereas an arginine/lysine ring that
287 tivity motif DEKA, line the walls of the ion-selectivity filter, whereas Glu and Lys are in positions
288 channels distinguish K(+) from Na(+) in the selectivity filter, which consists of four ion-binding s
289 nfigurations coexist within a K(+) channel's selectivity filter, which fully agrees with the water-K(
290 cific ion-mediated structural changes in the selectivity filter, which influences the permeability pr
291 tricted region of its open pore known as the selectivity filter, which is lined by four absolutely co
292 lular gate causes a structural change in the selectivity filter, which leads to a change in the ion o
293 e revealed a constricted conformation of the selectivity filter, which was proposed to represent the
294 wing water to penetrate the space behind the selectivity filter while simultaneously reducing the loc
295 vation by means of a local disruption in the selectivity filter, while severing the Tyr445-Thr439 H-b
296 the channel conductance is controlled at the selectivity filter, whose conformation depends on the ac
297 olvated monovalent ions permeate through the selectivity filter with comparable energetic barriers vi
298 a(2+)-dependent gating in MthK occurs at the selectivity filter with coupled movement of the intracel
299 ree energy for replacing Ca(2+) inside model selectivity filters with Na(+), we find that the nonmeta
300 t fluoride binds incoming protons within the selectivity filter, with excess protons shared with the