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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Expression, refolding, crystallization and preliminary crystallographic study of MHC H-2K(k) complexed with octapeptides and nonapeptides.
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Expression, refolding, crystallization and preliminary crystallographic study of MHC H-2K(k) complexed with octapeptides and nonapeptides.

机译：表情,重折叠,结晶初步的晶体研究MHC H-2K (k)包裹着八肽和九肽。

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摘要

Major histocompatibility complex (MHC) molecules are heterodimeric cell-surface receptors that play a crucial role in the cellular immune response by presenting epitope peptides to T-cell antigen receptors (TCR). Although the structural basis of the peptide-MHC binding mechanism is becoming better understood, it is still difficult to predict a binding mode for an MHC of unknown structure. Therefore, as the first stage of a TCR-MHC interaction study, the crystal structures of the mouse H-2K(k) molecule in complex with both an octapeptide from Influenza A virus and a nonapeptide from simian virus SV40 were solved. Here, the expression, refolding, purification and crystallization of the two complexes are reported. For the H-2K(k)-HA(259-266) complex, crystals were obtained via an extensive screen using a nanodrop-dispensing robot and diffracted to 2.5 A resolution. For the H-2K(k)-SV40(560-568) complex, microscopic needles were initially obtained and their size was improved by macroseeding and a stepwise increase in precipitant concentration. Diffraction data to a resolution of 3.0 A were collected at a synchrotron facility.
机译：主要组织相容性复合体(MHC)分子heterodimeric细胞表面受体细胞免疫发挥着至关重要的作用通过给t细胞表位肽的反应抗原受体(TCR)。peptide-MHC绑定机制的基础成为更好的理解,它仍然是困难的预测未知的MHC的绑定模式结构。TCR-MHC相互作用研究中,晶体结构鼠标H-2K (k)在复杂的分子一个从甲型流感病毒和八肽九肽从猴SV40病毒解决。在这里,表情,重折叠、净化和两个复合物的结晶报道。晶体获得通过一个广泛的屏幕使用nanodrop-dispensing机器人和衍射2.5解决方案。H-2K (k) sv40(560 - 568)复杂,微观针最初获得和他们的大小被macroseeding和逐步改善沉淀剂浓度的增加。衍射数据分辨率为3.0同步加速器装置收集。

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