1mhh: Difference between revisions

Revision as of 23:58, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mhh.png

Template:STRUCTURE 1mhh

Antibody-antigen complexAntibody-antigen complex

Template:ABSTRACT PUBMED 12221088

About this StructureAbout this Structure

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

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OCA

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 {{STRUCTURE_1mhh|  PDB=1mhh  |  SCENE=  }}
-'''Antibody-antigen complex'''
+===Antibody-antigen complex===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12221088}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12221088}}
 ==About this Structure==
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 [[Category: B cell superantigen]]
 [[Category: Immunoglobulin binding protein]]
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