C-13 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

被引：33

作者：

KATO, K ^{[1
]}

GOUDA, H ^{[1
]}

TAKAHA, W ^{[1
]}

YOSHINO, A ^{[1
]}

MATSUNAGA, C ^{[1
]}

ARATA, Y ^{[1
]}

机构：

[1] UNIV TOKYO, FAC PHARMACEUT SCI, TOKYO 113, JAPAN

来源：

FEBS LETTERS | 1993年 / 328卷 / 1-2期

基金：

日本科学技术振兴机构;

关键词：

IMMUNOGLOBULIN-G (MOUSE); FC; PROTEIN-A (STAPHYLOCOCCUS-AUREUS); C-13; NMR; PROTEIN PROTEIN INTERACTION;

D O I：

10.1016/0014-5793(93)80963-U

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 C-13 NMR spectroscopy. Mouse IgG1, IgG2a, and IgG2b proteins have been selectively labeled with C-13 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.

引用

页码：49 / 54

页数：6

共 25 条

[1] THE INTERACTION OF THE FACB FRAGMENT OF RABBIT ANTI-SHEEP RED-CELL IGG WITH GUINEA-PIG MACROPHAGES, AND HUMAN-MONOCYTES AND GRANULOCYTES [J].