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PMID: 8906788 Published · ppublish English Comment Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Structure of the complex between human T-cell receptor, viral peptide and HLA-A2.

Nature ·Vol. 384 ·No. 6605 ·1996-11-14 ·Pages 134-41

Garboczi DN, Ghosh P, Utz U, Fan QR, Biddison WE, Wiley DC

Abstract

Recognition by a T-cell antigen receptor (TCR) of peptide complexed with a major histocompatibility complex (MHC) molecule occurs through variable loops in the TCR structure which bury almost all the available peptide and a much larger area of the MHC molecule. The TCR fits diagonally across the MHC peptide-binding site in a surface feature common to all class I and class II MHC molecules, providing evidence that the nature of binding is general. A broadly applicable binding mode has implications for the mechanism of repertoire selection and the magnitude of alloreactions.

MeSH Terms
Crystallography, X-Ray Gene Products, tax/chemistry,immunology HLA-A2 Antigen/chemistry,immunology Human T-lymphotropic virus 1/chemistry,immunology Humans Immune Tolerance Immunoglobulin Fragments/chemistry Major Histocompatibility Complex Models, Molecular Protein Binding Protein Conformation Receptors, Antigen, T-Cell/chemistry,immunology Signal Transduction
Chemicals
Gene Products, tax HLA-A2 Antigen Immunoglobulin Fragments Receptors, Antigen, T-Cell
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Garboczi D N
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Ghosh P
Utz U
Fan Q R
Biddison W E
Wiley D C
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1996-11-14
Pages
134-41
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentOn
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