Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus
Housden, N.G., Harrison, S., Roberts, S.E., Beckingham, J.A., Graille, M., Stura, E. and Gore, M.G. (2003) Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus. Biochemical Society Transactions, 31, 716-718.
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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 k-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 k-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 k-chain than the second site.
|Keywords:||dissociation constant, immunoglobulin, mutant, sequence.|
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Divisions:||University Structure - Pre August 2011 > School of Biological Sciences
|Date Deposited:||07 Aug 2008|
|Last Modified:||12 May 2013 01:17|
|Contributors:||Housden, N.G. (Author)
Harrison, S. (Author)
Roberts, S.E. (Author)
Beckingham, J.A. (Author)
Graille, M. (Author)
Stura, E. (Author)
Gore, M.G. (Author)
|Date:||1 June 2003|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
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