金黄色葡萄球菌蛋白A的B片段与小鼠免疫球蛋白G的Fc片段在溶液中的相互作用模式的13C核磁共振研究。

13C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G.

作者信息

Kato K, Gouda H, Takaha W, Yoshino A, Matsunaga C, Arata Y

机构信息

Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.

出版信息

FEBS Lett. 1993 Aug 9;328(1-2):49-54. doi: 10.1016/0014-5793(93)80963-u.

DOI:10.1016/0014-5793(93)80963-u

PMID:8344434

Abstract

The mode of interaction of the B domain (FB) of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G (IgG) has been investigated by 13C NMR spectroscopy. Mouse IgG1, IgG2a, and IgG2b proteins have been selectively labeled with 13C at the carbonyl carbon of His, Met, Trp or Tyr residue and used to prepare the corresponding Fc fragments by limited proteolysis. Site-specific resonance assignments have been made for each of these Fc analogues. FB was reported to form two contacts (contact 1 and contact 2) with human Fc in the crystal [Biochemistry 20 (1981) 2361-2370]. Comparisons of the chemical shift data of the Fc fragments observed in the absence and presence of FB have led us to conclude that in solution contact 1 is responsible for the formation of the Fc-FB complexes.

摘要

利用13C核磁共振波谱法研究了葡萄球菌蛋白A的B结构域（FB）与小鼠免疫球蛋白G（IgG）的Fc片段之间的相互作用模式。小鼠IgG1、IgG2a和IgG2b蛋白已在His、Met、Trp或Tyr残基的羰基碳处用13C进行了选择性标记，并通过有限蛋白酶解用于制备相应的Fc片段。已对这些Fc类似物中的每一种进行了位点特异性共振归属。据报道，在晶体中FB与人类Fc形成两个接触点（接触点1和接触点2）[《生物化学》20（1981）2361 - 2370]。对在不存在和存在FB的情况下观察到的Fc片段的化学位移数据进行比较后，我们得出结论，在溶液中接触点1负责Fc - FB复合物的形成。