Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1.
The three-dimensional structure of the class II histocompatibility glycoprotein HLA-DR1 from human B-cell membranes has been determined by X-ray crystallography and is similar to that of class I HLA. Peptides are bound in an extended conformation that projects from both ends of an 'open-ended' antigen-binding groove. A prominent non-polar pocket into which an 'anchoring' peptide side chain fits is near one end of the binding groove. A dimer of the class II alpha beta heterodimers is seen in the crystal forms of HLA-DR1, suggesting class II HLA dimerization as a mechanism for initiating the cytoplasmic signalling events in T-cell activation.
Brown
J H
JH
Department of Biochemistry and Molecular Biology, Howard Hughes Medical Institute, Harvard University, Cambridge, Massachusetts 02138.
Jardetzky
T S
TS
Gorga
J C
JC
Stern
L J
LJ
Urban
R G
RG
Strominger
J L
JL
Wiley
D C
DC
D001402:B-Lymphocytes / Q000276:immunology; D001665:Binding Sites; D015704:CD4 Antigens / Q000378:metabolism; D002460:Cell Line; D003198:Computer Simulation; D015798:HLA-DR1 Antigen / Q000737:chemistry* / Q000378:metabolism; D015395:Histocompatibility Antigens Class I / Q000737:chemistry; D006801:Humans; D008213:Lymphocyte Activation; D008958:Models, Molecular; D010455:Peptides / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D015398:Signal Transduction; D013601:T-Lymphocytes / Q000276:immunology; D014961:X-Ray Diffraction
D015704:CD4 Antigens; D015798:HLA-DR1 Antigen; D015395:Histocompatibility Antigens Class I; D010455:Peptides