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1w0v

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[[Image:1w0v.gif|left|200px]]
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{{Seed}}
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[[Image:1w0v.png|left|200px]]
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{{STRUCTURE_1w0v| PDB=1w0v | SCENE= }}
{{STRUCTURE_1w0v| PDB=1w0v | SCENE= }}
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'''CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE SELF-PEPTIDE TIS FROM EGF-RESPONSE FACTOR 1'''
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===CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE SELF-PEPTIDE TIS FROM EGF-RESPONSE FACTOR 1===
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==Overview==
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The F pocket of major histocompatibility complex (in humans HLA) class I molecules accommodates the C terminus of the bound peptide. Residues forming this pocket exhibit considerable polymorphism, and a single difference (Asp116 in HLA-B*2705 and His116 in HLA-B*2709 heavy chains) confers differential association of these two HLA-B27 subtypes to the autoimmune disease ankylosing spondylitis. As peptide presentation by HLA molecules is of central importance for immune responses, we performed thermodynamic (circular dichroism, differential scanning calorimetry, fluorescence polarization) and X-ray crystallographic analyses of both HLA-B27 subtypes complexed with the epidermal growth factor response factor 1-derived self-peptide TIS (RRLPIFSRL) to understand the impact of the Asp116His exchange on peptide display. This peptide is known to be presented in vivo by both subtypes, and as expected for a self-peptide, TIS-reactive cytotoxic T lymphocytes are absent in the respective individuals. The thermodynamic analyses reveal that both HLA-B27:TIS complexes exhibit comparable, relatively high thermostability (Tm approximately 60 degrees C) and undergo multi-step unfolding reactions, with dissociation of the peptide in the first step. As shown by X-ray crystallography, only subtle structural differences between the subtypes were observed regarding the architecture of their F pockets, including the presence of distinct networks of water molecules. However, no consistent structural differences were found between the peptide presentation modes. In contrast to other peptides displayed by the two HLA-subtypes which show either structural or dynamical differences in their peptide presentation modes, the TIS-complexed HLA-B*2705 and HLA-B*2709 subtypes are an example for thermodynamic and structural equivalence, in agreement with functional data.
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The line below this paragraph, {{ABSTRACT_PUBMED_15713487}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15713487 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15713487}}
==About this Structure==
==About this Structure==
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:00:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:03:46 2008''

Revision as of 07:03, 29 July 2008

Image:1w0v.png

Template:STRUCTURE 1w0v

CRYSTAL STRUCTURE OF HLA-B*2705 COMPLEXED WITH THE SELF-PEPTIDE TIS FROM EGF-RESPONSE FACTOR 1

Template:ABSTRACT PUBMED 15713487

About this Structure

1W0V is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Thermodynamic and structural equivalence of two HLA-B27 subtypes complexed with a self-peptide., Hulsmeyer M, Welfle K, Pohlmann T, Misselwitz R, Alexiev U, Welfle H, Saenger W, Uchanska-Ziegler B, Ziegler A, J Mol Biol. 2005 Mar 11;346(5):1367-79. Epub 2005 Jan 28. PMID:15713487

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