1HSB

DIFFERENT LENGTH PEPTIDES BIND TO HLA-AW68 SIMILARLY AT THEIR ENDS BUT BULGE OUT IN THE MIDDLE

1HSB の概要

• エントリーDOI: 10.2210/pdb1hsb/pdb
• 分子名称: MHC class I antigen, Beta-2-microglobulin, BOUND PEPTIDE FRAGMENT, ... (6 entities in total)
• 機能のキーワード: histocompatibility antigen, immune system
• 細胞内の位置: Membrane; Single-pass type I membrane protein: A6YT91; Secreted: P61769
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 43423.10

構造登録者

Guo, H.-C.,Strominger, J.L.,Wiley, D.C. (登録日: 1993-03-30, 公開日: 1993-10-31, 最終更新日: 2024-10-30)

主引用文献

Guo, H.C.,Jardetzky, T.S.,Garrett, T.P.,Lane, W.S.,Strominger, J.L.,Wiley, D.C.
Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle.
Nature, 360:364-366, 1992

PubMed Abstract: We report here the determination and refinement to 1.9 A resolution by X-ray cryo-crystallography the structure of HLA-Aw68. The averaged image from the collection of bound, endogenous peptides clearly shows the atomic structure at the first three and last two amino acids in the peptides but no connected electron density in between. This suggests that bound peptides, held at both ends, take alternative pathways and could be of different lengths by bulging out in the middle. Peptides eluted from HLA-Aw68 include peptides of 9, 10 and 11 amino acids, a direct indication of the length heterogeneity of tightly bound peptides. Peptide sequencing shows relatively conserved 'anchor' residues at position 2 and the carboxy-terminal residue. Conserved binding sites for the peptide N and C termini at the ends of the class I major histocompatibility complex binding groove are apparently dominant in producing the long half-lives of peptide binding and the peptide-dependent stabilization of the class I molecule's structure.

PubMed: 1448153
DOI: 10.1038/360364a0

実験手法

X-RAY DIFFRACTION (1.9 Å)