The University of Southampton
University of Southampton Institutional Repository

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 The Journal of Biological Chemistry, 277, (49), pp. 47500-47506. (doi:10.1074/jbc.M206105200).

Record type: Article


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.

PDF findlow1_rae2008.pdf - Other
Restricted to Registered users only
Download (478kB)

More information

Submitted date: 19 June 2002
Published date: 8 September 2002
Keywords: human growth hormone, X-ray diffraction, peptosreptoococcus, crystal-structure, binding domain, straphylococcus-aureus, extracellular domain, FAB fragment, EPO receptor, human-IGG


Local EPrints ID: 24026
ISSN: 0021-9258
PURE UUID: ed12316c-cbcb-42a9-b8db-837fb51a9806

Catalogue record

Date deposited: 17 Mar 2006
Last modified: 17 Jul 2017 16:15

Export record



Author: Marc Graille
Author: Steven Harrison
Author: Matthew P. Crump
Author: Stuart C. Findlow
Author: Nicholas G. Housden
Author: Bruno H. Muller
Author: Nicole Battail-Poirot
Author: Geneviève Sibai
Author: Brian J. Sutton
Author: Michael J. Taussig
Author: Colette Jolivet-Reynaud
Author: Michael G. Gore
Author: Enrico A. Stura

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton:

ePrints Soton supports OAI 2.0 with a base URL of

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.