1mhh: Difference between revisions

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<StructureSection load='1mhh' size='340' side='right'caption='[[1mhh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1mhh' size='340' side='right'caption='[[1mhh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[1mhh]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Finegoldia_magna_ATCC_29328 Finegoldia magna ATCC 29328] 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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AEA:(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETIC+ACID'>AEA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhh OCA], [https://pdbe.org/1mhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mhh RCSB], [https://www.ebi.ac.uk/pdbsum/1mhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mhh ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhh OCA], [https://pdbe.org/1mhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mhh RCSB], [https://www.ebi.ac.uk/pdbsum/1mhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mhh ProSAT]</span></td></tr>
</table>
</table>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mhh ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mhh ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 1mhh" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Antibody 3D structures|Antibody 3D structures]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Finm2]]
[[Category: Finegoldia magna ATCC 29328]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Graille, M]]
[[Category: Graille M]]
[[Category: Stura, E A]]
[[Category: Stura EA]]
[[Category: Antibody-antigen complex]]
[[Category: B cell superantigen]]
[[Category: Immune system]]
[[Category: Immunoglobulin binding protein]]

Latest revision as of 11:36, 10 April 2024

Structure of P. magnus protein L mutant bound to a mouse FabStructure of P. magnus protein L mutant bound to a mouse Fab

Structural highlights

1mhh is a 6 chain structure with sequence from Finegoldia magna ATCC 29328 and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1mhh, resolution 2.10Å

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