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1tmc
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Class I major histocompatibility complex (MHC) molecules are ternary | + | 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. |
==Disease== | ==Disease== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Collins, E | + | [[Category: Collins, E J.]] |
| - | [[Category: Garboczi, D | + | [[Category: Garboczi, D N.]] |
| - | [[Category: Karpusas, M | + | [[Category: Karpusas, M N.]] |
| - | [[Category: Wiley, D | + | [[Category: Wiley, D C.]] |
[[Category: histocompatibility antigen]] | [[Category: histocompatibility antigen]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:07 2008'' |
Revision as of 13:15, 21 February 2008
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THE HTREE-DIMENSIONAL STRUCTURE OF A CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE MISSING THE ALPHA3 DOMAIN OF THE HEAVY CHAIN
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142800], Ankylosing spondylitis, susceptibility to, 1 OMIM:[142800], Hypoproteinemia, hypercatabolic OMIM:[109700], Stevens-Johnson syndrome, susceptibility to OMIM:[142800]
About this Structure
1TMC is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain., Collins EJ, Garboczi DN, Karpusas MN, Wiley DC, Proc Natl Acad Sci U S A. 1995 Feb 14;92(4):1218-21. PMID:7862664
Page seeded by OCA on Thu Feb 21 15:15:07 2008
