Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus
Immunoglobulin-binding domains: Protein L from Peptostreptococcus magnus
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.
dissociation constant, immunoglobulin, mutant, sequence.
716-718
Housden, N.G.
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Harrison, S.
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Roberts, S.E.
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Beckingham, J.A.
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Graille, M.
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Stura, E.
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Gore, M.G.
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1 June 2003
Housden, N.G.
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Harrison, S.
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Roberts, S.E.
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Beckingham, J.A.
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Graille, M.
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Stura, E.
a37324b9-b03c-42ca-b642-6ba684b864ee
Gore, M.G.
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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, .
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.
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More information
Published date: 1 June 2003
Keywords:
dissociation constant, immunoglobulin, mutant, sequence.
Identifiers
Local EPrints ID: 56623
URI: http://eprints.soton.ac.uk/id/eprint/56623
ISSN: 0300-5127
PURE UUID: 78cd2e08-2cde-458e-9f36-92d2066dd141
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Date deposited: 07 Aug 2008
Last modified: 08 Jan 2022 10:04
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Contributors
Author:
N.G. Housden
Author:
S. Harrison
Author:
S.E. Roberts
Author:
J.A. Beckingham
Author:
M. Graille
Author:
E. Stura
Author:
M.G. Gore
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