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Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1.
- Source :
-
Nature [Nature] 1993 Jul 01; Vol. 364 (6432), pp. 33-9. - Publication Year :
- 1993
-
Abstract
- 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.
- Subjects :
- B-Lymphocytes immunology
Binding Sites
CD4 Antigens metabolism
Cell Line
Computer Simulation
HLA-DR1 Antigen metabolism
Histocompatibility Antigens Class I chemistry
Humans
Lymphocyte Activation
Models, Molecular
Peptides metabolism
Protein Binding
Protein Conformation
Signal Transduction
T-Lymphocytes immunology
X-Ray Diffraction
HLA-DR1 Antigen chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0028-0836
- Volume :
- 364
- Issue :
- 6432
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 8316295
- Full Text :
- https://doi.org/10.1038/364033a0