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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >High-resolution structure of HLA-A*1101 in complex with SARS nucleocapsid peptide
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High-resolution structure of HLA-A*1101 in complex with SARS nucleocapsid peptide

机译：抗原* 1101的高分辨率结构复杂SARS病毒粒子肽

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摘要

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 angstrom 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.
机译：人类的mhc i分子抗原的结构*1101年在复杂nonameric肽(KTFPPTEPK)由x射线晶体学1.45埃分辨率。肽来源于冠核衣壳蛋白质位置362 - 370 (snp362 - 370)。守恒的冠和所有已知的隔离证实了体外peptide-binding吗研究是一个很好的中间粘合剂于* 0301和抗原* 1101的IC50值分别为70和186海里(Sylvester-Hvid等艾尔。(2004),组织抗原,63,395 - 400]。的残留peptide-binding衬里槽,于本院* 1101 - SNP362 - 370复杂其他已知的结构非常相似于* 1101和抗原* 6801。肽是一个17岁的氢键alpha-chain残留物和九水分子也紧密地绑定的peptide-binding槽。(Thr6p)不会使有效利用中间(E)的口袋里。是一个潜在的优化目标这个职位。Lys9p t细胞可识别。

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