2VAA

MHC CLASS I H-2KB HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND VESICULAR STOMATITIS VIRUS NUCLEOPROTEIN

「1VAA」から置き換えられました

2VAA の概要

• エントリーDOI: 10.2210/pdb2vaa/pdb
• 分子名称: MHC CLASS I H-2KB HEAVY CHAIN, BETA-2 MICROGLOBULIN, VESICULAR STOMATITIS VIRUS NUCLEOPROTEIN, ... (4 entities in total)
• 機能のキーワード: histocompatibility antigen, class i major histocompatibility complex, mhc i, mhc-peptide complex, complex (mhc i-peptide) complex, complex (mhc i/peptide)
• 由来する生物種: Mus musculus (house mouse); 詳細
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P01901; Secreted: P01887; Virion: P11212
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44308.76

構造登録者

Fremont, D.H.,Wilson, I.A. (登録日: 1994-11-01, 公開日: 1996-06-20, 最終更新日: 2024-10-23)

主引用文献

Fremont, D.H.,Matsumura, M.,Stura, E.A.,Peterson, P.A.,Wilson, I.A.
Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb.
Science, 257:919-927, 1992

PubMed Abstract: The x-ray structures of a murine MHC class I molecule (H-2Kb) 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-2Kb complexes were refined at 2.3 A for VSV-8 and 2.5 A for SEV-9. The structure of H-2Kb 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-2Kb 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-2Kb 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-2Kb are associated with peptide binding, and these synergistic movements may be an integral part of the T cell receptor recognition process.

PubMed: 1323877

実験手法

X-RAY DIFFRACTION (2.3 Å)