2xw9
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Crystal Structure of Complement Factor D mutant S183A== | |
| - | + | <StructureSection load='2xw9' size='340' side='right' caption='[[2xw9]], [[Resolution|resolution]] 1.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2xw9]] is a 1 chain structure with 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=2XW9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XW9 FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dst|1dst]], [[1dfp|1dfp]], [[1dic|1dic]], [[2xwa|2xwa]], [[1bio|1bio]], [[2xwb|2xwb]], [[1dsu|1dsu]], [[1hfd|1hfd]], [[1fdp|1fdp]], [[2xwj|2xwj]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Complement_factor_D Complement factor D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.46 3.4.21.46] </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=2xw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xw9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xw9 RCSB], [http://www.ebi.ac.uk/pdbsum/2xw9 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
[[http://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN]] Defects in CFD are the cause of complement factor D deficiency (CFDD) [MIM:[http://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. | [[http://www.uniprot.org/uniprot/CFAD_HUMAN CFAD_HUMAN]] Defects in CFD are the cause of complement factor D deficiency (CFDD) [MIM:[http://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 == | |
| - | ==Function== | + | |
[[http://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. | [[http://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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Activation of the complement cascade induces inflammatory responses and marks cells for immune clearance. In the central complement-amplification step, a complex consisting of surface-bound C3b and factor B is cleaved by factor D to generate active convertases on targeted surfaces. We present crystal structures of the pro-convertase C3bB at 4 angstrom resolution and its complex with factor D at 3.5 angstrom resolution. Our data show how factor B binding to C3b forms an open "activation" state of C3bB. Factor D specifically binds the open conformation of factor B through a site distant from the catalytic center and is activated by the substrate, which displaces factor D's self-inhibitory loop. This concerted proteolytic mechanism, which is cofactor-dependent and substrate-induced, restricts complement amplification to C3b-tagged target cells. | ||
| - | + | Structures of C3b in complex with factors B and D give insight into complement convertase formation.,Forneris F, Ricklin D, Wu J, Tzekou A, Wallace RS, Lambris JD, Gros P Science. 2010 Dec 24;330(6012):1816-20. PMID:21205667<ref>PMID:21205667</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Complement factor D]] | [[Category: Complement factor D]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Forneris, F | + | [[Category: Forneris, F]] |
| - | [[Category: Gros, P | + | [[Category: Gros, P]] |
| - | [[Category: Lambris, J D | + | [[Category: Lambris, J D]] |
| - | [[Category: Ricklin, D | + | [[Category: Ricklin, D]] |
| - | [[Category: Tzekou, A | + | [[Category: Tzekou, A]] |
| - | [[Category: Wallace, R S | + | [[Category: Wallace, R S]] |
| - | [[Category: Wu, J | + | [[Category: Wu, J]] |
[[Category: Alternative pathway]] | [[Category: Alternative pathway]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Immune system]] | [[Category: Immune system]] | ||
[[Category: Serine protease]] | [[Category: Serine protease]] | ||
Revision as of 13:34, 18 December 2014
Crystal Structure of Complement Factor D mutant S183A
| |||||||||||
