1dst: Difference between revisions

Revision as of 23:33, 30 June 2008

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File:1dst.png

Template:STRUCTURE 1dst

MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITYMUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY

Template:ABSTRACT PUBMED 7592653

About this StructureAbout this Structure

1DST is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jun 30 23:33:47 2008

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-'''MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY'''
+===MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7592653}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7592653 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7592653}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Serine protease]]
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