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==Overview==
==Overview==
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The products of the human leukocyte antigen subtypes HLA-B*2705 and, HLA-B*2709 differ only in residue 116 (Asp vs. His) within the peptide, binding groove but are differentially associated with the autoimmune, disease ankylosing spondylitis (AS); HLA-B*2705 occurs in AS-patients, whereas HLA-B*2709 does not. The subtypes also generate differential T, cell repertoires as exemplified by distinct T cell responses against the, self-peptide pVIPR (RRKWRRWHL). The crystal structures described here show, that pVIPR binds in an unprecedented dual conformation only to HLA-B*2705, molecules. In one binding mode, peptide pArg5 forms a salt bridge to, Asp116, connected with drastically different interactions between peptide, and heavy chain, contrasting with the second, conventional conformation, which is exclusively found in the case of B*2709. These subtype-dependent, differences in pVIPR binding link the emergence of dissimilar T cell, repertoires in individuals with HLA-B*2705 or HLA-B*2709 to the buried, Asp116/His116 polymorphism and provide novel insights into peptide, presentation by major histocompatibility antigens.
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The products of the human leukocyte antigen subtypes HLA-B*2705 and HLA-B*2709 differ only in residue 116 (Asp vs. His) within the peptide binding groove but are differentially associated with the autoimmune disease ankylosing spondylitis (AS); HLA-B*2705 occurs in AS-patients, whereas HLA-B*2709 does not. The subtypes also generate differential T cell repertoires as exemplified by distinct T cell responses against the self-peptide pVIPR (RRKWRRWHL). The crystal structures described here show that pVIPR binds in an unprecedented dual conformation only to HLA-B*2705 molecules. In one binding mode, peptide pArg5 forms a salt bridge to Asp116, connected with drastically different interactions between peptide and heavy chain, contrasting with the second, conventional conformation, which is exclusively found in the case of B*2709. These subtype-dependent differences in pVIPR binding link the emergence of dissimilar T cell repertoires in individuals with HLA-B*2705 or HLA-B*2709 to the buried Asp116/His116 polymorphism and provide novel insights into peptide presentation by major histocompatibility antigens.
==Disease==
==Disease==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Bettosini, F.]]
[[Category: Bettosini, F.]]
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[[Category: Fiorillo, M.T.]]
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[[Category: Fiorillo, M T.]]
[[Category: Hulsmeyer, M.]]
[[Category: Hulsmeyer, M.]]
[[Category: Saenger, W.]]
[[Category: Saenger, W.]]
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[[Category: mhc (major histocompatibility complex)]]
[[Category: mhc (major histocompatibility complex)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:57:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:57 2008''

Revision as of 12:17, 21 February 2008


1of2, resolution 2.20Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF HLA-B*2709 COMPLEXED WITH THE VASOACTIVE INTESTINAL PEPTIDE TYPE 1 RECEPTOR (VIPR) PEPTIDE (RESIDUES 400-408)

Contents

Overview

The products of the human leukocyte antigen subtypes HLA-B*2705 and HLA-B*2709 differ only in residue 116 (Asp vs. His) within the peptide binding groove but are differentially associated with the autoimmune disease ankylosing spondylitis (AS); HLA-B*2705 occurs in AS-patients, whereas HLA-B*2709 does not. The subtypes also generate differential T cell repertoires as exemplified by distinct T cell responses against the self-peptide pVIPR (RRKWRRWHL). The crystal structures described here show that pVIPR binds in an unprecedented dual conformation only to HLA-B*2705 molecules. In one binding mode, peptide pArg5 forms a salt bridge to Asp116, connected with drastically different interactions between peptide and heavy chain, contrasting with the second, conventional conformation, which is exclusively found in the case of B*2709. These subtype-dependent differences in pVIPR binding link the emergence of dissimilar T cell repertoires in individuals with HLA-B*2705 or HLA-B*2709 to the buried Asp116/His116 polymorphism and provide novel insights into peptide presentation by major histocompatibility antigens.

Disease

Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Hypoproteinemia, hypercatabolic OMIM:[109700], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]

About this Structure

1OF2 is a Protein complex structure of sequences from Homo sapiens with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Dual, HLA-B27 subtype-dependent conformation of a self-peptide., Hulsmeyer M, Fiorillo MT, Bettosini F, Sorrentino R, Saenger W, Ziegler A, Uchanska-Ziegler B, J Exp Med. 2004 Jan 19;199(2):271-81. PMID:14734527

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