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'''MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY''' | '''MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY''' | ||
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[[Category: Narayana, S V.L.]] | [[Category: Narayana, S V.L.]] | ||
[[Category: Volanakis, J E.]] | [[Category: Volanakis, J E.]] | ||
[[Category: | [[Category: Complement activating enzyme]] | ||
[[Category: | [[Category: Factor d]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Serine protease]] | ||
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Revision as of 14:13, 2 May 2008
MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY
OverviewOverview
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.
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 Fri May 2 14:13:54 2008