ライフサイエンスコーパス: B30.2 domain

1 tyrophilin (BTN)3A1, using its intracellular B30.2 domain.

2 by direct interactions through the PRY/SPRY/B30.2 domain.

3 caspase-1 at Asp330, a site remote from the B30.2 domain.

4 nd that is located close to the start of the B30.2 domain.

5 artite motif (the RBCC domain) followed by a B30.2 domain.

6 surface-exposed elements on one face of the B30.2 domain.

7 ce of mutations reside in pyrin's C-terminal B30.2 domain.

8 t this interaction depends on the TRIM5alpha B30.2 domain.

9 es largely consistent with the origin of the B30.2 domain.

10 n of the retroviral capsid by the TRIM5alpha B30.2 domain.

11 variable regions (v1, v2, and v3) within the B30.2 domain.

12 variable regions (v1, v2, v3, and v4) in the B30.2 domain.

13 ce and "knockin" mice harboring mutant human B30.2 domains.

14 y of TRIM5alphas containing mixed or mutated B30.2 domains.

15 uential RING finger, B Box, coiled-coil, and B30.2 domains.

16 asic pocket and surrounding V regions of the B30.2 domain abrogated prenyl pyrophosphate-induced prol

17 el revealed that the variable regions of the B30.2 domain are present as loops located on one side of

18 hanges were incorporated into the TRIM5alpha B30.2 domain at discrete time points during the evolutio

19 d on separate exons and are separated from a B30.2 domain by a variable number of very short exons, 2

20 idues in the v1 region of the TRIM5alpha(hu) B30.2 domain can modulate capsid binding and restriction

21 se-1 with the deduced structure of the pyrin B30.2 domain corroborated both the interaction and the i

22 N3A1) protein that contains an intracellular B30.2 domain critical to pAg reactivity.

23 Using a B30.2-domain-encoding DNA probe so derived from the hema

24 ing of the human RBCC domain followed by the B30.2 domain from various primates was constructed.

25 al di-leucine motif, located proximal to the B30.2 domain in the BTN3A1 cytoplasmic tail.

26 HEPES, 150 mM NaCl, pH 7.4) to the PRY/SPRY/B30.2 domain in the cytoplasmic region of bovine BTN1A1.

27 n activity dependent on the integrity of the B30.2 domain, in particular primate species.

28 The B30.2 domain is thought to be involved in determination

29 diminished stimulation, suggesting that the B30.2 domain may interact with a second protein.

30 We proposed that the intracellular B30.2 domain of BTN3A1 binds prenyl pyrophosphates, resu

31 functional approaches that the intracellular B30.2 domain of BTN3A1 directly binds pAg through a posi

32 nyl pyrophosphate binds to the intracellular B30.2 domain of BTN3A1 with an affinity of 1.1 muM, wher

33 ious work has shown that the C-terminal SPRY/B30.2 domain of dimeric TRIM5alpha binds directly to vir

34 human paralogs, BTN2A1 or BTN3A1, or to the B30.2 domain of human RoRet (TRIM 38), a protein in the

35 Missense mutations in the C-terminal B30.2 domain of pyrin cause familial Mediterranean fever

36 The C-terminal B30.2 domain of pyrin is necessary and sufficient for th

37 n this pocket that, when introduced into the B30.2 domain of the nonstimulatory BTN3A3 isoform, trans

38 , a model for the molecular structure of the B30.2 domain of TRIM5alpha was developed.

39 llular domains, a model of the intracellular B30.2 domain predicts a basic pocket on its binding surf

40 s a new unique member of the rapidly growing B30.2 domain proteins.

41 conformational change in the position of the B30.2 domain relative to the juxtamembrane (JM) region.

42 ration of arginine 332 in the TRIM5alpha(hu) B30.2 domain to proline, the residue found in rhesus mon

43 Tandem duplications in the TRIM5alpha B30.2 domain v1 region of African green monkeys are also

44 der monkey TRIM5alpha, which has an expanded B30.2 domain v3 region due to a tandem triplication, pot

45 tive of selection bordering these particular B30.2 domain variable elements.

46 involving particularly the carboxyl-terminal B30.2 domain, was a notable feature.

47 , encoding a RING finger-like protein with a B30.2 domain, was discovered during an in silico search

48 et TRIM5alpha gene exon 8, which encodes the B30.2 domain, was found to be pseudogenized.

49 production by interaction of its C-terminal B30.2 domain with the catalytic domains of caspase-1.