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1dst

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Revision as of 07:55, 16 October 2019

MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY

Structural highlights

1dst 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.
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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Complement factor D is a serine protease regulated by a novel mechanism that depends on conformational changes rather than cleavage of a zymogen for expression of proteolytic activity. The conformational changes are presumed to be induced by the single natural substrate, C3bB, and to result in reversible reorientation of the catalytic center and of the substrate binding site of factor D, both of which have atypical conformations. Here we report that replacement of Ser94, Thr214, and Ser215 of factor D (chymotrypsinogen numbering has been used for comparison purposes) with the corresponding residues of trypsin, Tyr, Ser, and Trp, is sufficient to induce substantially higher catalytic activity associated with a typical serine protease alignment of the catalytic triad residues His57, Asp102, and Ser195. These results provide a partial structural explanation for the low reactivity of "resting-state" factor D toward synthetic substrates.

Crystal structure of a complement factor D mutant expressing enhanced catalytic activity.,Kim S, Narayana SV, Volanakis JE J Biol Chem. 1995 Oct 13;270(41):24399-405. PMID:7592653^[1]

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

References

↑ Kim S, Narayana SV, Volanakis JE. Crystal structure of a complement factor D mutant expressing enhanced catalytic activity. J Biol Chem. 1995 Oct 13;270(41):24399-405. PMID:7592653

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dst"

@@ Line 1: / Line 1: @@
 ==MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY==
-<StructureSection load='1dst' size='340' side='right' caption='[[1dst]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1dst' size='340' side='right'caption='[[1dst]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1dst]] 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=1DST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DST FirstGlance]. <br>
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 1dst" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Complement factor 3D structures|Complement factor 3D structures]]
 == References ==
 <references/>
@@ Line 36: / Line 39: @@
 [[Category: Complement factor D]]
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Narayana, S V.L]]
 [[Category: Volanakis, J E]]

1dst

From Proteopedia

Revision as of 07:55, 16 October 2019

MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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