1dsu: Difference between revisions

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-{{Seed}}
-[[Image:1dsu.png|left|200px]]
-<!--
+==HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME==
-The line below this paragraph, containing "STRUCTURE_1dsu", creates the "Structure Box" on the page.
+<StructureSection load='1dsu' size='340' side='right'caption='[[1dsu]], [[Resolution|resolution]] 2.00&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'>[[1dsu]] is a 2 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=1DSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DSU 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&#8491;</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=1dsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsu OCA], [https://pdbe.org/1dsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dsu RCSB], [https://www.ebi.ac.uk/pdbsum/1dsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dsu ProSAT]</span></td></tr>
-{{STRUCTURE_1dsu|  PDB=1dsu  |  SCENE=  }}
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN] Defects in CFD are the cause of complement factor D deficiency (CFDD) [MIM:[https://omim.org/entry/613912 613912]. CFDD is an immunologic disorder characterized by increased susceptibility to bacterial infections, particularly Neisseria infections, due to a defect in the alternative complement pathway.
+== Function ==
+[https://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN] Factor D cleaves factor B when the latter is complexed with factor C3b, activating the C3bbb complex, which then becomes the C3 convertase of the alternate pathway. Its function is homologous to that of C1s in the classical pathway.
+== 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/ds/1dsu_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=1dsu ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Factor D, an essential enzyme for the activation of the alternative pathway of the complement system, belongs to the serine protease superfamily. The crystal structure of the enzyme was solved by a combination of multiple isomorphous replacement and molecular replacement methods. The present model was refined to an R-factor of 18.8% using 23,681 observed reflections between 7.5 and 2.0 A resolution, with a root-mean-square deviation from standard bond lengths of 0.016 A. The two non-crystallographically related molecules in the triclinic unit cell have distinctive active site conformations. The protein has the general structural fold of a serine protease, but there are several unique amino acid substitutions resulting in significant alterations in the critical loops responsible for catalysis and substrate specificity in serine proteases. Factor D is the first complement serine protease whose three-dimensional structure has been determined.
-===HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME===
+Structure of human factor D. A complement system protein at 2.0 A resolution.,Narayana SV, Carson M, el-Kabbani O, Kilpatrick JM, Moore D, Chen X, Bugg CE, Volanakis JE, DeLucas LJ J Mol Biol. 1994 Jan 14;235(2):695-708. PMID:8289289<ref>PMID:8289289</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1dsu" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_8289289}}, 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 8289289 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_8289289}}
+__TOC__
+</StructureSection>
-==About this Structure==
-DSU is a [[Single protein]] 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=1DSU OCA].
-==Reference==
-Structure of human factor D. A complement system protein at 2.0 A resolution., Narayana SV, Carson M, el-Kabbani O, Kilpatrick JM, Moore D, Chen X, Bugg CE, Volanakis JE, DeLucas LJ, J Mol Biol. 1994 Jan 14;235(2):695-708. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8289289 8289289]
-[[Category: Complement factor D]]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Delucas, L J.]]
+[[Category: Delucas LJ]]
-[[Category: Narayana, S V.L.]]
+[[Category: Narayana SVL]]
-[[Category: Volanakis, J E.]]
+[[Category: Volanakis JE]]
-[[Category: Complement activating enzyme]]
-[[Category: Hydrolase]]
-[[Category: Serine protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:33:53 2008''