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Protein Sci. 1996 Apr;5(4):553-64.

Complement factor D, a novel serine protease.

Author information

1
Department of Medicine, University of Alabama at Birmingham 35294, USA. jvolanakis@medinfo.dom.uab.edu

Abstract

Factor D is unique among serine proteases in that it requires neither enzymatic cleavage for expression of proteolytic activity nor inactivation by a serpin for its control. Regulation of factor D activity is instead attained by a novel mechanism that depends on reversible conformational changes for expression and control of catalytic activity. These conformational changes are believed to be induced by the single natural substrate, C3bB, and to result in realignment of the catalytic triad, the specificity pocket, and the nonspecific substrate binding site, all of which have atypical conformations. Mutational studies have defined structural determinants responsible for these unique structural features of factor D and for the resultant low reactivity with synthetic esters.

PMID:
8845746
PMCID:
PMC2143395
DOI:
10.1002/pro.5560050401
[Indexed for MEDLINE]
Free PMC Article

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