1mhh
From Proteopedia
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| - | [[Image:1mhh.gif|left|200px]] | + | [[Image:1mhh.gif|left|200px]] |
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| - | '''Antibody-antigen complex''' | + | {{Structure |
| + | |PDB= 1mhh |SIZE=350|CAPTION= <scene name='initialview01'>1mhh</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Antibody-antigen complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MHH is a [ | + | 1MHH is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] and [http://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]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12221088 12221088] |
[[Category: Finegoldia magna]] | [[Category: Finegoldia magna]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
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[[Category: immunoglobulin binding protein]] | [[Category: immunoglobulin binding protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:43:26 2008'' |
Revision as of 10:43, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Antibody-antigen complex
Overview
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 Structure
1MHH is a Protein complex structure of sequences from Finegoldia magna and Mus musculus. Full crystallographic information is available from OCA.
Reference
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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