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[[Image:1mhh.gif|left|200px]]


{{Structure
==Structure of P. magnus protein L mutant bound to a mouse Fab==
|PDB= 1mhh |SIZE=350|CAPTION= <scene name='initialview01'>1mhh</scene>, resolution 2.1&Aring;
<StructureSection load='1mhh' size='340' side='right'caption='[[1mhh]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=AEA:(2-AMINO-2-CARBAMOYL-ETHYLSULFANYL)-ACETIC+ACID'>AEA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
<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>
|ACTIVITY=  
</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>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=[[1hez|1HEZ]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mhh OCA], [http://www.ebi.ac.uk/pdbsum/1mhh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mhh RCSB]</span>
== Evolutionary Conservation ==
}}
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mh/1mhh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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>


'''Antibody-antigen complex'''
==See Also==
 
*[[Antibody 3D structures|Antibody 3D structures]]
 
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
==Overview==
__TOC__
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.
</StructureSection>
 
[[Category: Finegoldia magna ATCC 29328]]
==About this Structure==
[[Category: Large Structures]]
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==
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: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Graille M]]
[[Category: Graille, M.]]
[[Category: Stura EA]]
[[Category: Stura, E A.]]
[[Category: antibody-antigen complex]]
[[Category: b cell superantigen]]
[[Category: immunoglobulin binding protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:16:06 2008''

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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