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1 dsRBDs 1, 3 and 4 bind dsRNA in vitro, but dsRBDs 2 and
4 o varieties of dsRBD exist: canonical Type A dsRBDs interact with dsRNA, while non-canonical Type B d
5 dsRBD by assessing the binding of dsRBM1 and dsRBD to a series of dsRNA sequences ranging from 15 to
6 etect low-affinity binding of the kinase and dsRBD constructs in solution, indicating that these doma
8 eract with dsRNA, while non-canonical Type B dsRBDs lack RNA-binding residues and instead interact wi
11 ynamics and structures of the free and bound dsRBD reveals that slow-timescale dynamics in the alpha1
12 dsRBDs 1, 3 and 4 bind dsRNA in vitro, but dsRBDs 2 and 5 do not, although dsRBD2 does bind dsRNA w
20 t the end of the Rnt1p dsRNA-binding domain (dsRBD) and the guanine nucleotide in the second position
21 KR has a double-stranded RNA-binding domain (dsRBD) composed of two copies of the dsRNA binding motif
22 7) in the Aa-RNase III dsRNA-binding domain (dsRBD) directly interacts with a proximal box base pair.
24 functional domains: a dsRNA binding domain (dsRBD) for siRNA docking and a pH-dependent polyhistidin
27 that its double-stranded RNA binding domain (dsRBD) is the limiting sequence required for this intera
28 with the double-stranded RNA-binding domain (dsRBD) motif although there is little (<10%) sequence ho
29 tructure of the 20 kDa dsRNA-binding domain (dsRBD) of human PKR, which provides the first three-dime
30 ding by the C-terminal dsRNA-binding domain (dsRBD) of RNase III, indicating that EB perturbs substra
32 ein kinase (PKR) has a dsRNA-binding domain (dsRBD) that contains two tandem copies of the dsRNA-bind
34 h as the double-stranded RNA binding domain (dsRBD), the hnRNP K homology (KH) domain and the RNP mot
38 ive double-stranded (ds)RNA-binding domains (dsRBDs) and a short region within an insertion that spli
40 f viral dsRNAs to two dsRNA-binding domains (dsRBDs) in PKR leads to relief of an inhibitory region a
41 ein that contains two dsRNA-binding domains (dsRBDs) in tandem, is vital for nuclear maturation of pr
42 Two double-stranded RNA binding domains (dsRBDs) in the N-terminal half of PKR are thought to bin
43 , whose double-stranded RNA-binding domains (dsRBDs) interact with the A-form geometry of double-stra
44 randed RNA (dsRNA) by dsRNA-binding domains (dsRBDs) is involved in a large number of biological and
46 rboring double-stranded RNA binding domains (dsRBDs) play diverse functional roles such as RNA locali
47 s were created in the dsRNA binding domains (dsRBDs) that abolished all RNA binding, as tested for tw
48 to PKR double-stranded RNA-binding domains (dsRBDs) were determined by isothermal titration calorime
51 The nature of these interactions explains dsRBD specificity for dsRNA (over ssRNA or dsDNA) and th
56 etermined the solution structure of the free dsRBD used in the previously determined RNA-bound struct
57 dimers require two subunits with functional dsRBDs for binding to a dsRNA substrate and then for edi
63 rticipates in the regulated translocation of dsRBD proteins to the cytoplasm where they interact with
68 operties of pY are not identical to those of dsRBDs, as the postulated RNA-binding site in pY does no
69 , these results suggest that this particular dsRBD-dsRNA interaction produces little to no change in
70 We report the solution structure of Rnt1p dsRBD complexed to the 5' terminal hairpin of one of its
73 etermined the backbone dynamics of the Rnt1p dsRBD in the free and AGAA hairpin-bound states using NM
76 fically modified each of the dsRBMs of PKR's dsRBD with the hydroxyl radical generator EDTA small mid
77 A resolution crystal structure of the second dsRBD of Xenopus laevis RNA-binding protein A complexed
79 Purified, mutant proteins lacking single dsRBDs still bind RNA efficiently, demonstrating that no
80 ex shows surprising similarity to the tandem dsRBDs from an adenosine-to-inosine editing enzyme, ADAR
82 inant class of dsRNA-binding domains, termed dsRBDs, that are found in a large number of eukaryotic a
86 ce electrostatic potential in HI0257 and the dsRBD family reveals significant differences in the loca
87 The most immediate differences between the dsRBD and HI0257 structures are that (1) HI0257 has a la
91 te whether conformational flexibility in the dsRBD regulates the binding specificity, we determined t
92 gle of about 30 degrees to each other in the dsRBD, and (3) HI0257 lacks the extended loop commonly s
94 rm of Escherichia coli RNase III lacking the dsRBD (RNase III[DeltadsRBD]) can accurately cleave smal
97 We have characterized the function of the dsRBD by assessing the binding of dsRBM1 and dsRBD to a
99 ond-to-millisecond timescale dynamics of the dsRBD suggests that helix alpha1 undergoes conformationa
102 domain (i) can function independently of the dsRBD, (ii) is dsRNA-specific, and (iii) participates in
106 ral model showing how Trn1 can recognize the dsRBD-NLS and how dsRNA binding can interfere with Trn1
108 n are non-equivalent; regions other than the dsRBD stem-loops of inhibitory RNA are required for inhi
109 l and biochemical analyses indicate that the dsRBD and N-terminal domains (NTDs) of Rnt1p function as
111 alpha1-beta1 hinge result in changes to the dsRBD stability and RNA-binding affinity and cause defec
113 As of cellular and viral origins bind to the dsRBD, leading to either activation or inhibition of PKR
115 The binding sites on inhibitor RNAs and the dsRBDs of PKR have been mapped by NMR chemical shift per
118 nction of double-stranded RNA binding to the dsRBDs of native PKR is to promote dimerization and acti
122 A binding protein (TRBP) consisting of three dsRBDs, which functions in HIV replication, protein kina
125 ructure of the linker region between the two dsRBDs that differs from the flexible linker connecting
126 the interfacial interactions between the two dsRBDs, we ran extensive MD simulations of isolated dsRB
130 e of the dsRBD-NLS, which reveals an unusual dsRBD fold extended by an additional N-terminal alpha-he
131 d by molecular-dynamics simulations in which dsRBD-dsRNA interactions generate only modest bending of
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