Evidence for plasticity and structural mimicry at the immunoglobulin light chain-protein L interface

Graille, Marc, Harrison, Steven, Crump, Matthew P. , Findlow, Stuart C. , Housden, Nicholas G., Muller, Bruno H., Battail-Poirot, Nicole, Sibai, Geneviève, Sutton, Brian J., Taussig, Michael J., Jolivet-Reynaud, Colette, Gore, Michael G. and Stura, Enrico A. (2002) Evidence for plasticity and structural mimicry at the immunoglobulin light chain-protein L interface. Journal of Biological Chemistry, 277, (49), 47500-47506. (doi:10.1074/jbc.M206105200).


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Original Publication URL: http://dx.doi.org/10.1074/jbc.M206105200


The multidomain bacterial surface protein L (PpL) is a virulence factor expressed by only 10% of Peptostreptococcus magnus strains, and its expression is correlated with bacterial vaginosis. The molecular basis for its ability to recognize 60% of mammalian immunoglobulin light chain variable regions (V-L) has been described recently by x-ray crystallography, which suggested the presence of two V-L binding sites on each protein L domain (Graille, M., Stura, E. A., Housden, N.G., Beekingham, J.A., Bottomley, S. P., Beale, D., Taussig, M.J., Sutton, B.J., Gore, M. G., and Charbonnier, J. (2001) Structure, 679-687). Here, we report the crystal structure at 2.1 Angstrom resolution of a protein L mutant complexed to an Fab' fragment with only 50% of the VL residues interacting with PpL site 1 conserved. Comparison of the site 1 interface from both structures shows how protein L is able to accommodate these sequence differences and therefore bind to a large repertoire of Ig. The x-ray structure and NMR results confirm the existence of two V-L binding sites on a single protein L domain. These sites exhibit a remarkable structural mimicry of growth factors binding to their receptors. This could explain the protein L superantigenic activity on human B lymphocytes.

Item Type: Article
Digital Object Identifier (DOI): doi:10.1074/jbc.M206105200
ISSNs: 0021-9258 (print)
Related URLs:
Keywords: human growth hormone, X-ray diffraction, peptosreptoococcus, crystal-structure, binding domain, straphylococcus-aureus, extracellular domain, FAB fragment, EPO receptor, human-IGG
Subjects: Q Science > Q Science (General)
Divisions : University Structure - Pre August 2011 > School of Biological Sciences
ePrint ID: 24026
Accepted Date and Publication Date:
8 September 2002Published
19 June 2002Submitted
Date Deposited: 17 Mar 2006
Last Modified: 31 Mar 2016 11:45
URI: http://eprints.soton.ac.uk/id/eprint/24026

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