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2HN7

HLA-A*1101 in complex with HBV peptide homologue

Summary for 2HN7
Entry DOI10.2210/pdb2hn7/pdb
DescriptorHLA class I histocompatibility antigen, A-11 alpha chain, Beta-2-microglobulin, DNA polymerase PEPTIDE HOMOLOGUE, ... (5 entities in total)
Functional Keywordspeptide-mhc-complex, major histocompatibility complex class i, mhc-i, human leukocyte antigen, hla, immunoglobulin family, hepatitis b virus, hbv, immune system
Biological sourceHomo sapiens (human)
More
Cellular locationMembrane; Single-pass type I membrane protein: P13746
Secreted: P61769
Total number of polymer chains3
Total formula weight45086.87
Authors
Blicher, T. (deposition date: 2006-07-12, release date: 2006-11-28, Last modification date: 2024-10-16)
Primary citationBlicher, T.,Kastrup, J.S.,Pedersen, L.O.,Buus, S.,Gajhede, M.
Structure of HLA-A*1101 in complex with a hepatitis B peptide homologue.
Acta Crystallogr.,Sect.F, 62:1179-1184, 2006
Cited by
PubMed Abstract: 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).
PubMed: 17142892
DOI: 10.1107/S1744309106044228
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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