2bzm: Difference between revisions
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New page: left|200px<br /> <applet load="2bzm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bzm" /> '''SOLUTION STRUCTURE OF THE PRIMARY HOST RECO... |
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== | ==Solution structure of the primary host recognition region of complement factor H== | ||
Mutations and polymorphisms in the regulator of complement activation, factor H, have been linked to atypical hemolytic uremic syndrome (aHUS), membranoproliferative glomerulonephritis, and age-related macular | <StructureSection load='2bzm' size='340' side='right'caption='[[2bzm]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bzm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BZM FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 26 models</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=2bzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bzm OCA], [https://pdbe.org/2bzm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bzm RCSB], [https://www.ebi.ac.uk/pdbsum/2bzm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bzm ProSAT]</span></td></tr> | |||
</table> | |||
== 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/bz/2bzm_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2bzm ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Mutations and polymorphisms in the regulator of complement activation, factor H, have been linked to atypical hemolytic uremic syndrome (aHUS), membranoproliferative glomerulonephritis, and age-related macular degeneration. Many aHUS patients carry mutations in the two C-terminal modules of factor H, which normally confer upon this abundant 155-kDa plasma glycoprotein its ability to selectively bind self-surfaces and prevent them from inappropriately triggering the complement cascade via the alternative pathway. In the current study, the three-dimensional solution structure of the C-terminal module pair of factor H has been determined. A binding site for a fully sulfated heparin-derived tetrasaccharide has been delineated using chemical shift mapping and the C3d/C3b-binding site inferred from sequence comparisons and computational docking. The resultant information allows assessment of the likely consequences of aHUS-associated amino acid substitutions in this critical region of factor H. It is striking that, excepting those likely to perturb the three-dimensional structure, aHUS-associated missense mutations congregate in the polyanion-binding site delineated in this study, thus potentially disrupting a vital mechanism for control of complement on self-surfaces in the microvasculature of the kidney. It is intriguing that a single nucleotide polymorphism predisposing to age-related macular degeneration occupies another region of factor H that harbors a polyanion-binding site. | |||
Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in three-dimensional structure.,Herbert AP, Uhrin D, Lyon M, Pangburn MK, Barlow PN J Biol Chem. 2006 Jun 16;281(24):16512-20. Epub 2006 Mar 13. PMID:16533809<ref>PMID:16533809</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2bzm" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Complement factor 3D structures|Complement factor 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Barlow | [[Category: Barlow PN]] | ||
[[Category: Herbert | [[Category: Herbert AP]] | ||
[[Category: Lyon | [[Category: Lyon M]] | ||
[[Category: Pangburn | [[Category: Pangburn MK]] | ||
[[Category: Uhrin | [[Category: Uhrin D]] | ||
