1nyo: Difference between revisions
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<StructureSection load='1nyo' size='340' side='right' caption='[[1nyo]], [[NMR_Ensembles_of_Models | 38 NMR models]]' scene=''> | <StructureSection load='1nyo' size='340' side='right' caption='[[1nyo]], [[NMR_Ensembles_of_Models | 38 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1nyo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1nyo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NYO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NYO FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mpt70/mpb70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mpt70/mpb70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nyo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1nyo RCSB], [http://www.ebi.ac.uk/pdbsum/1nyo PDBsum], [http://www.topsan.org/Proteins/TBSGC/1nyo TOPSAN]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nyo OCA], [http://pdbe.org/1nyo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nyo RCSB], [http://www.ebi.ac.uk/pdbsum/1nyo PDBsum], [http://www.topsan.org/Proteins/TBSGC/1nyo TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1nyo" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bloemink, M J]] | [[Category: Bloemink, M J]] | ||
[[Category: Carr, M D]] | [[Category: Carr, M D]] | ||
Revision as of 07:31, 11 September 2015
Solution structure of the antigenic TB protein MPT70/MPB70Solution structure of the antigenic TB protein MPT70/MPB70
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe closely related mycobacteria responsible for tuberculosis produce an unusually high number of secreted proteins, many of which are clearly implicated in pathogenesis and protective immunity. Falling within this category are the closely related proteins MPB70 and MPB83. The structure of MPB70 reveals a complex and novel bacterial fold, which has clear structural homology to the two C-terminal FAS1 domains of the cell adhesion protein fasciclin I, whose structures were reported very recently. Assessment of the surface features of MPB70, the sequence divergence between MPB70 and MPB83, the conservation of residues across a group of FAS1 domains, and the locations of disease-inducing mutations in betaig-h3 strongly suggests that MPB70 and MPB83 contain two functional surfaces on opposite faces, which are probably involved in binding to host cell proteins. This analysis also suggests that these functional surfaces are retained in the FAS1 proteins associated with mediating interactions between cells and the extracellular matrix (fasciclin I, periostin, and betaig-h3) and furthermore that some of the human corneal disease-inducing substitutions identified in betaig-h3 will perturb interactions at these sites. Solution structure of the Mycobacterium tuberculosis complex protein MPB70: from tuberculosis pathogenesis to inherited human corneal desease.,Carr MD, Bloemink MJ, Dentten E, Whelan AO, Gordon SV, Kelly G, Frenkiel TA, Hewinson RG, Williamson RA J Biol Chem. 2003 Oct 31;278(44):43736-43. Epub 2003 Aug 12. PMID:12917404[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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