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| - | [[Image:1s9v.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1s9v| PDB=1s9v | SCENE= }} | | {{STRUCTURE_1s9v| PDB=1s9v | SCENE= }} |
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| - | '''Crystal structure of HLA-DQ2 complexed with deamidated gliadin peptide'''
| + | ===Crystal structure of HLA-DQ2 complexed with deamidated gliadin peptide=== |
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| - | ==Overview==
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| - | Celiac disease, also known as celiac sprue, is a gluten-induced autoimmune-like disorder of the small intestine, which is strongly associated with HLA-DQ2. The structure of DQ2 complexed with an immunogenic epitope from gluten, QLQPFPQPELPY, has been determined to 2.2-A resolution by x-ray crystallography. The glutamate at P6, which is formed by tissue transglutaminase-catalyzed deamidation, is an important anchor residue as it participates in an extensive hydrogen-bonding network involving Lys-beta71 of DQ2. The gluten peptide-DQ2 complex retains critical hydrogen bonds between the MHC and the peptide backbone despite the presence of many proline residues in the peptide that are unable to participate in amide-mediated hydrogen bonds. Positioning of proline residues such that they do not interfere with backbone hydrogen bonding results in a reduction in the number of registers available for gluten peptides to bind to MHC class II molecules and presumably impairs the likelihood of establishing favorable side-chain interactions. The HLA association in celiac disease can be explained by a superior ability of DQ2 to bind the biased repertoire of proline-rich gluten peptides that have survived gastrointestinal digestion and that have been deamidated by tissue transglutaminase. Finally, surface-exposed proline residues in the proteolytically resistant ligand were replaced with functionalized analogs, thereby providing a starting point for the design of orally active agents for blocking gluten-induced toxicity.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15020763}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15020763 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15020763}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hla-dq2]] | | [[Category: Hla-dq2]] |
| | [[Category: Immune system]] | | [[Category: Immune system]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:27:55 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:01:33 2008'' |
Revision as of 11:01, 29 July 2008
Template:STRUCTURE 1s9v
Crystal structure of HLA-DQ2 complexed with deamidated gliadin peptide
Template:ABSTRACT PUBMED 15020763
About this Structure
1S9V is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease., Kim CY, Quarsten H, Bergseng E, Khosla C, Sollid LM, Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4175-9. Epub 2004 Mar 12. PMID:15020763
Page seeded by OCA on Tue Jul 29 14:01:33 2008
