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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Description/Abstract
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.
| Item Type: | Article |
|---|---|
| ISSNs: | 0300-5127 (print) |
| Related URLs: | |
| Keywords: | dissociation constant, immunoglobulin, mutant, sequence. |
| Subjects: | Q Science > QH Natural history > QH301 Biology |
| Divisions: | University Structure - Pre August 2011 > School of Biological Sciences |
| Item ID: | 56623 |
| 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 |
| Status: | Published |
| URI: | http://eprints.soton.ac.uk/id/eprint/56623 |
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