2hn7

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Revision as of 23:27, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2hn7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hn7, resolution 1.60Å" /> '''HLA-A*1101 in compl...)
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File:2hn7.gif


2hn7, resolution 1.60Å

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HLA-A*1101 in complex with HBV peptide homologue

OverviewOverview

A high-resolution structure of the human MHC-I molecule HLA-A*1101 is, presented in which it forms a complex with a sequence homologue of a, peptide that occurs naturally in hepatitis B virus DNA polymerase. The, sequence of the bound peptide is AIMPARFYPK, while that of the, corresponding natural peptide is LIMPARFYPK. The peptide does not make, efficient use of the middle E pocket for binding, which leads to a rather, superficial and exposed binding mode for the central peptide residues., Despite this, the peptide binds with high affinity (IC50 of 31 nM).

DiseaseDisease

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 StructureAbout this Structure

2HN7 is a Protein complex structure of sequences from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue., Blicher T, Kastrup JS, Pedersen LO, Buus S, Gajhede M, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1179-84. Epub 2006 Nov 4. PMID:17142892

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