Three-dimensional solution structure of an immunoglobulin light chain-binding domain of protein L. Comparison with the IgG-binding domains of protein G

Biochemistry ◽  
1994 ◽  
Vol 33 (47) ◽  
pp. 14011-14017 ◽  
Author(s):  
Mats Wikstroem ◽  
Torbjoern Drakenberg ◽  
Sture Forsen ◽  
Ulf Sjoebring ◽  
Lars Bjoerck
Keyword(s):  
Light Chain ◽  
Solution Structure ◽  
Three Dimensional ◽  
Binding Domain ◽  
Protein G ◽  
Immunoglobulin Light Chain ◽  
Protein L ◽  
Dimensional Solution ◽  
Binding Domains ◽  
Igg Binding

Three-dimensional solution structure of a single zinc finger DNA-binding domain

Science ◽  
1989 ◽  
Vol 245 (4918) ◽  
pp. 635-637 ◽  
Author(s):  
M. Lee ◽  
G. Gippert ◽  
K. Soman ◽  
D. Case ◽  
P. Wright
Keyword(s):  
Dna Binding ◽  
Zinc Finger ◽  
Solution Structure ◽  
Three Dimensional ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Dimensional Solution

scholarly journals Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus

2003 ◽  
Vol 31 (3) ◽  
pp. 716-718 ◽  
Author(s):  
N.G. Housden ◽  
S. Harrison ◽  
S.E. Roberts ◽  
J.A. Beckingham ◽  
M. Graille ◽  
...  
Keyword(s):  
Binding Sites ◽  
Protein A ◽  
Cell Wall Protein ◽  
Protein G ◽  
Protein L ◽  
Heavy Chains ◽  
Binding Domains ◽  
Peptostreptococcus Magnus ◽  
Immunoglobulin Binding

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 CH2-CH3 heavy chains, while Protein L binds exclusively to the VL domain of the κ-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 κ-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 κ-chain than the second site.

Three-Dimensional Solution Structure ofSaccharomyces cerevisiaeReduced Iso-1-cytochromec†

Biochemistry ◽  
1996 ◽  
Vol 35 (43) ◽  
pp. 13788-13796 ◽  
Author(s):  
Paolo Baistrocchi ◽  
Lucia Banci ◽  
Ivano Bertini ◽  
Paola Turano ◽  
Kara L. Bren ◽  
...  
Keyword(s):  
Solution Structure ◽  
Three Dimensional ◽  
Dimensional Solution

Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G

2016 ◽  
Vol 128 (33) ◽  
pp. 9719-9722 ◽  
Author(s):  
Supriya Pratihar ◽  
T. Michael Sabo ◽  
David Ban ◽  
R. Bryn Fenwick ◽  
Stefan Becker ◽  
...  
Keyword(s):  
Binding Domain ◽  
Recognition Site ◽  
Protein G ◽  
Antibody Recognition ◽  
The Third ◽  
Igg Binding ◽  
Kinetics Of

The Third IgG-Binding Domain from Streptococcal Protein G

1994 ◽  
Vol 243 (5) ◽  
pp. 906-918 ◽  
Author(s):  
Jeremy P. Derrick ◽  
Dale B. Wigley
Keyword(s):  
Binding Domain ◽  
Protein G ◽  
The Third ◽  
Igg Binding ◽  
Streptococcal Protein G
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