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| Article Authors: | E J Collins; D N Garboczi; M N Karpusas; D C Wiley |
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| Article Title: | The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain. |
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| Reference ID: | 1013620 |
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| Abstract: | Class I major histocompatibility complex (MHC) molecules are ternary complexes of the soluble serum protein beta 2-microglobulin, MHC heavy chain, and bound peptide. The first two domains (alpha 1, alpha 2) of the heavy chain create the peptide binding cleft and the surface that contacts the T-cell receptor. The third domain (alpha 3) associates with the T-cell co-receptor, CD8, during T-cell recognition. Here we describe the x-ray crystal structure of a human class I MHC molecule, HLA-Aw68, from which the alpha 3 domain has been proteolytically removed. The resulting molecule shows no gross morphological changes compared to the intact protein. A decameric peptide complexed with the intact HLA-Aw68 is seen to bind to the proteolized molecule in the conventional manner, demonstrating that the alpha 3 domain is not required for the structural integrity of the molecule or for peptide binding. |
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| Affiliations: | Department of Molecular and Cellular Biology, Howard Hughes Medical Institute, Harvard University, Cambridge, MA 02138. |
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| Date: | 1995 |
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| Reference Type: | Literature |
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| PubMed ID: | 7862664 |
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| Journal: | Proc Natl Acad Sci U S A |
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| Journal Volume: | 92 |
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| Article Pages: | 1218-21 |
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| Journal ISSN: | 1091-6490 |
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| Article Chemical List: | HLA-A Antigens;HLA-A*68 antigen;Peptide Fragments |
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| Article MeSH List: | Amino Acid Sequence; Cell Line; Crystallography, X-Ray; HLA-A Antigens(chemistry; metabolism); Humans; Hydrolysis; Molecular Sequence Data; Peptide Fragments(chemistry; metabolism); Protein Binding; Protein Structure, Tertiary |
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| Curation Last Updated: | 2011-08-24 00:17:35 |
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