1X7Q

Crystal structure of HLA-A*1101 with sars nucleocapsid peptide

Summary for 1X7Q

• Entry DOI: 10.2210/pdb1x7q/pdb
• Descriptor: HLA class I histocompatibility antigen, A-11 alpha chain, Beta-2-microglobulin, SARS NUCLEOCAPSID PEPTIDE, ... (6 entities in total)
• Functional Keywords: peptide-mhc-complex, major histocompatibility complex class i, mhc-i, human leukocyte antigen, hla, immunoglobulin family, sars, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P13746; Secreted: P61769; Virion: P59595
• Total number of polymer chains: 3
• Total formula weight: 45582.27

Authors

Blicher, T.,Kastrup, J.S.,Buus, S.,Gajhede, M. (deposition date: 2004-08-16, release date: 2005-08-02, Last modification date: 2024-10-23)

Primary citation

Blicher, T.,Kastrup, J.S.,Buus, S.,Gajhede, M.
High-resolution structure of HLA-A*1101 in complex with SARS nucleocapsid peptide.
Acta Crystallogr.,Sect.D, 61:1031-1040, 2005

PubMed Abstract: The structure of the human MHC-I molecule HLA-A*1101 in complex with a nonameric peptide (KTFPPTEPK) has been determined by X-ray crystallography to 1.45 A resolution. The peptide is derived from the SARS-CoV nucleocapsid protein positions 362-370 (SNP362-370). It is conserved in all known isolates of SARS-CoV and has been verified by in vitro peptide-binding studies to be a good to intermediate binder to HLA-A*0301 and HLA-A*1101, with IC50 values of 70 and 186 nM, respectively [Sylvester-Hvid et al. (2004), Tissue Antigens, 63, 395-400]. In terms of the residues lining the peptide-binding groove, the HLA-A*1101-SNP362-370 complex is very similar to other known structures of HLA-A*1101 and HLA-A*6801. The SNP362-370 peptide is held in place by 17 hydrogen bonds to the alpha-chain residues and by nine water molecules which are also tightly bound in the peptide-binding groove. Thr6 of the peptide (Thr6p) does not make efficient use of the middle (E) pocket. For vaccine development, there seems to be a potential for optimization targeted at this position. All residues except Thr2p and Lys9p are accessible for T-cell recognition.

PubMed: 16041067
DOI: 10.1107/S0907444905013090

Experimental method

X-RAY DIFFRACTION (1.45 Å)