1FZM

MHC CLASS I NATURAL MUTANT H-2KBM8 HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND VESICULAR STOMATITIS VIRUS NUCLEOPROTEIN

1FZM の概要

• エントリーDOI: 10.2210/pdb1fzm/pdb
• 関連するPDBエントリー: 1FZJ 1FZK 1FZO 2vaa 2vab
• 分子名称: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-B ALPHA CHAIN, PROTEIN (BETA-2-MICROGLOBULIN), PROTEIN (NUCLEOCAPSID PROTEIN), ... (9 entities in total)
• 機能のキーワード: major histocompatibility complex peptide-mhc, immune system
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 45583.92

構造登録者

Rudolph, M.G.,Speir, J.A.,Brunmark, A.,Mattsson, N.,Jackson, M.R.,Peterson, P.A.,Teyton, L.,Wilson, I.A. (登録日: 2000-10-03, 公開日: 2001-03-28, 最終更新日: 2024-11-20)

主引用文献

Rudolph, M.G.,Speir, J.A.,Brunmark, A.,Mattsson, N.,Jackson, M.R.,Peterson, P.A.,Teyton, L.,Wilson, I.A.
The crystal structures of K(bm1) and K(bm8) reveal that subtle changes in the peptide environment impact thermostability and alloreactivity.
Immunity, 14:231-242, 2001

PubMed Abstract: The K(bm1) and K(bm8) natural mutants of the murine MHC class I molecule H-2K(b) were originally identified by allograft rejection. They also bind viral peptides VSV8 and SEV9 with high affinity, but their peptide complexes have substantially decreased thermostability, and the K(bm1) complexes do not elicit alloreactive T cell responses. Crystal structures of the four mutant complexes at 1.7-1.9 A resolution are similar to the corresponding wild-type K(b) structures, except in the vicinity of the mutated residues, which alter the electrostatic potential, topology, hydrogen bonding, and local water structure of the peptide binding groove. Thus, these natural K(b) mutations define the minimal perturbations in the peptide environment that alter antigen presentation to T cells and abolish alloreactivity.

PubMed: 11290333
DOI: 10.1016/S1074-7613(01)00105-4

実験手法

X-RAY DIFFRACTION (1.8 Å)