2hn7
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| , resolution 1.60Å | |||||||
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| Ligands: | |||||||
| Gene: | HLA-A, HLAA (Homo sapiens), B2M (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 disease associated with this structure: Hypoproteinemia, hypercatabolic OMIM:[109700]
About this StructureAbout this Structure
2HN7 is a Protein complex structure of sequences from Homo sapiens. 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 Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1179-84. Epub 2006 Nov 4. PMID:17142892
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