1mhh
Antibody-antigen complex
|
OverviewOverview
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., Beckingham, J. A., Bottomley, S. P., Beale, D., Taussig, M. J., Sutton, B., J., Gore, M. G., and Charbonnier, J. (2001) Structure 9, 679-687). Here, we report the crystal structure at 2.1 A resolution of a protein L mutant, complexed to an Fab' fragment with only 50% of the V(L) 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.
About this StructureAbout this Structure
1MHH is a Protein complex structure of sequences from Finegoldia magna and Mus musculus with EDO as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Evidence for plasticity and structural mimicry at the immunoglobulin light chain-protein L interface., Graille M, Harrison S, Crump MP, Findlow SC, Housden NG, Muller BH, Battail-Poirot N, Sibai G, Sutton BJ, Taussig MJ, Jolivet-Reynaud C, Gore MG, Stura EA, J Biol Chem. 2002 Dec 6;277(49):47500-6. Epub 2002 Sep 8. PMID:12221088
Page seeded by OCA on Sun Nov 18 09:36:42 2007