1mhh

<table><tr><td colspan='2'>[[1mhh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Finm2 Finm2] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MHH FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AEA:(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETIC+ACID'>AEA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hez|1hez]]</div></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12221088</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1mhh" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Finm2]]

[[Category: Graille, M]]

[[Category: Stura, E A]]

[[Category: Immunoglobulin binding protein]]