2ok5: Difference between revisions

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-{{Seed}}
-[[Image:2ok5.png|left|200px]]
-<!--
+==Human Complement factor B==
-The line below this paragraph, containing "STRUCTURE_2ok5", creates the "Structure Box" on the page.
+<StructureSection load='2ok5' size='340' side='right'caption='[[2ok5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2ok5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OK5 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-{{STRUCTURE_2ok5|  PDB=2ok5  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ok5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ok5 OCA], [https://pdbe.org/2ok5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ok5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ok5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ok5 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/CFAB_HUMAN CFAB_HUMAN] Defects in CFB are a cause of susceptibility to hemolytic uremic syndrome atypical type 4 (AHUS4) [MIM:[https://omim.org/entry/612924 612924]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.<ref>PMID:17182750</ref> <ref>PMID:20513133</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/CFAB_HUMAN CFAB_HUMAN] Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B-lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes.
+== 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/ok/2ok5_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=2ok5 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Factor B is the central protease of the complement system of immune defense. Here, we present the crystal structure of human factor B at 2.3-A resolution, which reveals how the five-domain proenzyme is kept securely inactive. The canonical activation helix of the Von Willebrand factor A (VWA) domain is displaced by a helix from the preceding domain linker. The two helices conformationally link the scissile-activation peptide and the metal ion-dependent adhesion site required for binding of the ligand C3b. The data suggest that C3b binding displaces the three N-terminal control domains and reshuffles the two central helices. Reshuffling of the helices releases the scissile bond for final proteolytic activation and generates a new interface between the VWA domain and the serine protease domain. This allosteric mechanism is crucial for tight regulation of the complement-amplification step in the immune response.
-===Human Complement factor B===
+Factor B structure provides insights into activation of the central protease of the complement system.,Milder FJ, Gomes L, Schouten A, Janssen BJ, Huizinga EG, Romijn RA, Hemrika W, Roos A, Daha MR, Gros P Nat Struct Mol Biol. 2007 Mar;14(3):224-8. Epub 2007 Feb 25. PMID:17310251<ref>PMID:17310251</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2ok5" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_17310251}}, adds the Publication Abstract to the page
+*[[Complement factor 3D structures|Complement factor 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 17310251 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_17310251}}
+__TOC__
+</StructureSection>
-==About this Structure==
-OK5 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OK5 OCA].
-==Reference==
-<ref group="xtra">PMID:17310251</ref><references group="xtra"/>
-[[Category: Alternative-complement-pathway C3/C5 convertase]]
 [[Category: Homo sapiens]]
-[[Category: Daha, M R.]]
+[[Category: Large Structures]]
-[[Category: Gomes, L.]]
+[[Category: Daha MR]]
-[[Category: Gros, P.]]
+[[Category: Gomes L]]
-[[Category: Hemrika, W.]]
+[[Category: Gros P]]
-[[Category: Huizinga, E G.]]
+[[Category: Hemrika W]]
-[[Category: Janssen, B J.C.]]
+[[Category: Huizinga EG]]
-[[Category: Milder, F J.]]
+[[Category: Janssen BJC]]
-[[Category: Romijn, R A.]]
+[[Category: Milder FJ]]
-[[Category: Roos, A.]]
+[[Category: Romijn RA]]
-[[Category: Schouten, A.]]
+[[Category: Roos A]]
-[[Category: Ccp domain]]
+[[Category: Schouten A]]
-[[Category: Pro-enzyme]]
-[[Category: Serine protease domain,von willebrand factor-a domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 13:58:37 2009''