2xw9

From Proteopedia

(Difference between revisions)

Revision as of 12:23, 22 July 2020

Crystal Structure of Complement Factor D mutant S183A

Structural highlights

2xw9 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1dst, 1dfp, 1dic, 2xwa, 1bio, 2xwb, 1dsu, 1hfd, 1fdp, 2xwj
Activity:	Complement factor D, with EC number 3.4.21.46
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Forneris F, Ricklin D, Wu J, Tzekou A, Wallace RS, Lambris JD, Gros P. Structures of C3b in complex with factors B and D give insight into complement convertase formation. Science. 2010 Dec 24;330(6012):1816-20. PMID:21205667 doi:10.1126/science.1195821

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2xw9"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Complement Factor D mutant S183A==
-<StructureSection load='2xw9' size='340' side='right' caption='[[2xw9]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
+<StructureSection load='2xw9' size='340' side='right'caption='[[2xw9]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2xw9]] is a 1 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=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>
+<table><tr><td colspan='2'>[[2xw9]] is a 1 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=2XW9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XW9 FirstGlance]. <br>
-</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>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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://pdbe.org/2xw9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xw9 RCSB], [http://www.ebi.ac.uk/pdbsum/2xw9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xw9 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xw9 OCA], [http://pdbe.org/2xw9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xw9 RCSB], [http://www.ebi.ac.uk/pdbsum/2xw9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xw9 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 24: / Line 24: @@
 ==See Also==
-*[[Complement factor|Complement factor]]
+*[[Complement factor 3D structures|Complement factor 3D structures]]
 == References ==
 <references/>
@@ Line 31: / Line 31: @@
 [[Category: Complement factor D]]
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Forneris, F]]
 [[Category: Gros, P]]

2xw9

From Proteopedia

Revision as of 12:23, 22 July 2020

Crystal Structure of Complement Factor D mutant S183A

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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