1B3J

STRUCTURE OF THE MHC CLASS I HOMOLOG MIC-A, A GAMMADELTA T CELL LIGAND

1B3J の概要

• エントリーDOI: 10.2210/pdb1b3j/pdb
• 分子名称: MHC CLASS I HOMOLOG MIC-A, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: hc i homolog, human mica, mica, immunology, mhc, gamma-delta-tcr, glycoprotein, signa immunoglobulin fold, t-cell, immune system
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32024.64

構造登録者

Li, P.,Willie, S.,Bauer, S.,Morris, D.,Spies, T.,Strong, R. (登録日: 1998-12-11, 公開日: 1999-07-09, 最終更新日: 2024-10-09)

主引用文献

Li, P.,Willie, S.T.,Bauer, S.,Morris, D.L.,Spies, T.,Strong, R.K.
Crystal structure of the MHC class I homolog MIC-A, a gammadelta T cell ligand.
Immunity, 10:577-584, 1999

PubMed Abstract: The major histocompatibility complex (MHC) class I homolog MIC-A functions as a stress-inducible antigen that is recognized by a subset of gammadelta T cells independent of beta2-microglobulin and bound peptides. Its crystal structure reveals a dramatically altered MHC class I fold, both in detail and overall domain organization. The only remnant of a peptide-binding groove is a small cavity formed as the result of disordering a large section of one of the groove-defining helices. Loss of beta2-microglobulin binding is due to a restructuring of the interaction interfaces. Structural mapping of sequence variation suggests potential receptor binding sites on the underside of the platform on the side opposite of the surface recognized by alphabeta T cell receptors on MHC class I-peptide complexes.

PubMed: 10367903
DOI: 10.1016/S1074-7613(00)80057-6

実験手法

X-RAY DIFFRACTION (3 Å)