5nat
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Complement factor D in complex with the inhibitor (S)-Pyrrolidine-1,2-dicarboxylic acid 1-[(1-methyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide]== | |
| - | + | <StructureSection load='5nat' size='340' side='right' caption='[[5nat]], [[Resolution|resolution]] 1.17Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5nat]] 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=5NAT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NAT FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8RT:(2~{S})-~{N}1-(1-methylindol-3-yl)-~{N}2-[3-(trifluoromethyloxy)phenyl]pyrrolidine-1,2-dicarboxamide'>8RT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |
| - | [[Category: | + | <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=5nat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nat OCA], [http://pdbe.org/5nat PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nat RCSB], [http://www.ebi.ac.uk/pdbsum/5nat PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nat ProSAT]</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. | ||
| + | == 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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Complement factor D]] | ||
| + | [[Category: Homo sapiens]] | ||
[[Category: Ostermann, N]] | [[Category: Ostermann, N]] | ||
| - | [[Category: | + | [[Category: Sweeney, A Mac]] |
| + | [[Category: Hydrolase]] | ||
Revision as of 07:29, 21 March 2018
Complement factor D in complex with the inhibitor (S)-Pyrrolidine-1,2-dicarboxylic acid 1-[(1-methyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide]
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