Immunoglobulin-binding domains:: Protein L from Peptostreptococcus magnus

被引:1
|
作者
Housden, NG
Harrison, S
Roberts, SE
Beckingham, JA
Graille, M
Stura, E
Gore, MG
机构
[1] Univ Southampton, Inst Biomol Sci, Div Biochem & Mol Biol, Southampton SO16 7PX, Hants, England
[2] CEA, DIEP, Lab Struct Prot, F-91191 Gif Sur Yvette, France
关键词
dissociation constant; immunoglobulin; mutant; sequence;
D O I
10.1042/BST0310716
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
Protein L is a multidomain cell-wall protein isolated from Peptostreptococcus magnus. it belongs to a group of proteins that contain repeated domains that are able to bind to Igs without stimulating an immune response, the most characterized of this group being Protein A (Staphylococcus aureus) and Protein G (Streptococcus). Both of these proteins bind predominantly to the interface of C(H)2-C(H)3 heavy chains, while Protein L binds exclusively to the V-L domain of the kappa-chain. The function of these proteins in vivo is not clear but it is thought that they enable the bacteria to evade the host's immune system. Two binding sites for kappa-chain on a single Ig-binding domain from Protein L have recently been reported and we give evidence that one site has a 25-55-fold higher affinity for kappa-chain than the second site.
引用
收藏
页码:716 / 718
页数:3
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