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人类重链病蛋白Riv的晶体与人Fc片段晶体是同晶型的:免疫球蛋白铰链区构象灵活性的进一步证据。

Crystals of the human heavy chain disease protein Riv and human Fc fragment are isomorphous: further evidence for conformational flexibility in the hinge region of immunoglobulins.

作者信息

Mariuzza R A, Poljak R J, Mihaesco C, Mihaesco E

出版信息

J Mol Biol. 1983 Apr 15;165(3):559-61. doi: 10.1016/s0022-2836(83)80220-4.

Abstract

Protein Riv is a human gamma 1 heavy chain disease immunoglobulin variant with a deletion of the entire VH and CH1 domains and consisting of most of the hinge region plus the CH2 and CH3 domains. Crystals of this protein are orthorhombic, belonging to the space group P2(1)2(1)2(1), with a = 80.1 A, b = 145.5 A, c = 50.1 A. These crystals are shown to be isomorphous with crystals of a human Fc fragment, indicating that the hinge region and the initial part of the CH2 domain of protein Riv do not assume a unique conformation in the crystalline state.

摘要

蛋白质Riv是一种人类γ1重链病免疫球蛋白变体,其整个VH和CH1结构域缺失,由大部分铰链区以及CH2和CH3结构域组成。该蛋白质的晶体为正交晶系,属于空间群P2(1)2(1)2(1),a = 80.1 Å,b = 145.5 Å,c = 50.1 Å。这些晶体被证明与人类Fc片段的晶体同晶型,表明蛋白质Riv的铰链区和CH2结构域的起始部分在晶体状态下不具有独特的构象。

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