Structure of the human class I histocompatibility antigen, HLA-A2

Nature. 1987 Oct 8-14;329(6139):506-12. doi: 10.1038/329506a0.

Abstract

The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are paired in a novel manner, and the region distal from the membrane is a platform of eight antiparallel beta-strands topped by alpha-helices. A large groove between the alpha-helices provides a binding site for processed foreign antigens. An unknown 'antigen' is found in this site in crystals of purified HLA-A2.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antigens / metabolism
  • Binding Sites
  • Computer Graphics
  • Glycoproteins / metabolism
  • HLA Antigens* / metabolism
  • HLA-A2 Antigen
  • Humans
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • beta 2-Microglobulin / metabolism

Substances

  • Antigens
  • Glycoproteins
  • HLA Antigens
  • HLA-A2 Antigen
  • Membrane Proteins
  • beta 2-Microglobulin