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首页> 外文期刊>Journal of Molecular Biology >Crystal structure of an Fab fragment in complex with a meningococcal serosubtype antigen and a protein G domain.
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Crystal structure of an Fab fragment in complex with a meningococcal serosubtype antigen and a protein G domain.

机译：与脑膜炎球菌血清亚型抗原和蛋白G结构域复合的Fab片段的晶体结构。

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摘要

Many pathogens present highly variable surface proteins to their host as a means of evading immune responses. The structure of a peptide antigen corresponding to the subtype P1.7 variant of the porin PorA from the human pathogen Neisseria meningitidis was determined by solution of the X-ray crystal structure of the ternary complex of the peptide (ANGGASGQVK) in complex with a Fab fragment and a domain from streptococcal protein G to 1.95 A resolution. The peptide adopted a beta-hairpin structure with a type I beta-turn between residues Gly4P and Gly7P, the conformation of the peptide being further stabilised by a pair of hydrogen bonds from the side-chain of Asn2P to main-chain atoms in Val9P. The antigen binding site within the Fab formed a distinct crevice lined by a high proportion of apolar amino acids. Recognition was supplemented by hydrogen bonds from heavy chain residues Thr50H, Asp95H, Leu97H and Tyr100H to main-chain and side-chain atoms in the peptide. Complementarity-determining region (CDR) 3 of the heavy chain was responsible for approximately 50 % of the buried surface area formed by peptide-Fab binding, with the remainder made up from CDRs 1 and 3 of the light chain and CDRs 1 and 2 of the heavy chain. Knowledge of the structures of variable surface antigens such as PorA is an essential prerequisite to a molecular understanding of antigenic variation and its implications for vaccine design. Copyright 1999 Academic Press.
机译：许多病原体将高度可变的表面蛋白呈现给宿主，以逃避免疫反应。通过将肽的三元复合物（ANGGASGQVK）与Fab复合的溶液的X射线晶体结构确定，确定与来自人类病原体脑膜炎奈瑟氏球菌的孔蛋白PorA亚型P1.7变体相对应的肽抗原的结构。片段和一个从链球菌蛋白G到1.95 A分辨率的结构域。该肽采用β-发夹结构，在残基Gly4P和Gly7P之间具有I型β转角，该肽的构象通过从Asn2P的侧链到Val9P的主链原子的一对氢键进一步稳定。 Fab内的抗原结合位点形成了由高比例的非极性氨基酸排列的独特缝隙。通过从重链残基Thr50H，Asp95H，Leu97H和Tyr100H到肽中主链和侧链原子的氢键来补充识别。重链的互补决定区（CDR）3约占肽-Fab结合形成的掩埋表面积的50％，其余部分由轻链的CDR 1和3以及轻链的CDR 1和2组成。重链。了解可变表面抗原（例如PorA）的结构是对抗原变异及其对疫苗设计的意义进行分子理解的必要前提。版权所有1999，学术出版社。

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