CRYSTAL-STRUCTURES OF 2 VIRAL PEPTIDES IN COMPLEX WITH MURINE MHC CLASS-I H-2K(B)
CRYSTAL-STRUCTURES OF 2 VIRAL PEPTIDES IN COMPLEX WITH MURINE MHC CLASS-I H-2K(B)
复制标题
DOI：
10.1126/science.1323877
复制
发表时间：
1992-08-14
期刊：
影响因子：
56.9
通讯作者：
WILSON, IA
中科院分区：
文献类型：
--
作者：
FREMONT, DH;MATSUMURA, M;WILSON, IA
研究了小鼠MHC I类分子（H-2K(b)）与两种不同的病毒肽复合物的x射线结构，这两种病毒肽分别来自水疱性口炎病毒核蛋白（52-59）VSV-8和仙台病毒核蛋白（324-332）SEV-9。H-2K(b)配合物在vesv -8和SEV-9分别为2.3埃和2.5埃。H-2K(b)的结构表现出与人类HLA I类的高度相似性，尽管个别结构域可能有轻微的改变。这两种肽都以延伸的构象结合，它们的大部分表面都埋在H-2K(b)结合槽中。非聚体肽与八聚体保持相同的氨基端和羧基端相互作用，主要是通过在其他构象的中心插入一个凸起。大多数特异性相互作用发生在H-2K(b)的侧链原子和肽的主链原子之间。这种结合方案在很大程度上解释了肽序列的巨大多样性，这些序列与I类分子具有高亲和力。H-2K(b)中微小但显著的构象变化与肽结合有关，这些协同运动可能是T细胞受体识别过程的一个组成部分。
The x-ray structures of a murine MHC class I molecule (H-2K(b)) were determined in complex with two different viral peptides, derived from the vesicular stomatitis virus nucleoprotein(52-59), VSV-8, and the Sendai virus nucleoprotein(324-332), SEV-9. The H-2K(b) complexes were refined at 2.3 angstrom for VSV-8 and 2.5 angstrom for SEV-9. The structure of H-2K(b) exhibits a high degree of similarity with human HLA class I, although the individual domains can have slightly altered dispositions. Both peptides bind in extended conformations with most of their surfaces buried in the H-2K(b) binding groove. The nonamer peptide maintains the same amino- and carboxyl-terminal interactions as the octamer primarily by the insertion of a bulge in the center of an otherwise beta-conformation. Most of the specific interactions are between side-chain atoms of H-2K(b) and main-chain atoms of peptide. This binding scheme accounts in large part for the enormous diversity of peptide sequences that bind with high affinity to class I molecules. Small but significant conformational changes in H-2K(b) are associated with peptide binding, and these synergistic movements may be an integral part of the T cell receptor recognition process.