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1b3j
From Proteopedia
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STRUCTURE OF THE MHC CLASS I HOMOLOG MIC-A, A GAMMADELTA T CELL LIGAND
Overview
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.
About this Structure
1B3J is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the MHC class I homolog MIC-A, a gammadelta T cell ligand., Li P, Willie ST, Bauer S, Morris DL, Spies T, Strong RK, Immunity. 1999 May;10(5):577-84. PMID:10367903
Page seeded by OCA on Thu Feb 21 11:51:07 2008
Categories: Homo sapiens | Single protein | Bauer, S. | Li, P. | Morris, D. | Spies, T. | Strong, R. | Willie, S. | Gamma-delta-tcr | Glycoprotein | Hc i homolog | Human mica | Immunology | Mhc | Mica | Signa immunoglobulin fold | T-cell
