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==Crystal structure of Complement Factor D mutant R202A after ensemble refinement== | |||
<StructureSection load='4cbo' size='340' side='right' caption='[[4cbo]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
=== | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cbo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBO 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">[[4cbn|4cbn]]</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=4cbo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbo RCSB], [http://www.ebi.ac.uk/pdbsum/4cbo 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. | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Complement factor D]] | [[Category: Complement factor D]] | ||
[[Category: Burnley, B T | [[Category: Human]] | ||
[[Category: Forneris, F | [[Category: Burnley, B T]] | ||
[[Category: Gros, P | [[Category: Forneris, F]] | ||
[[Category: Gros, P]] | |||
[[Category: Ensemble refinement]] | [[Category: Ensemble refinement]] | ||
[[Category: Factor d]] | [[Category: Factor d]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 20:35, 21 December 2014
Crystal structure of Complement Factor D mutant R202A after ensemble refinementCrystal structure of Complement Factor D mutant R202A after ensemble refinement
Structural highlights
Disease[CFAD_HUMAN] Defects in CFD are the cause of complement factor D deficiency (CFDD) [MIM: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[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. |
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