Complement factor D, a novel serine protease.
Protein Sci
; 5(4): 553-64, 1996 Apr.
Article
en En
| MEDLINE
| ID: mdl-8845746
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.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Serina Endopeptidasas
/
Factor D del Complemento
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Protein Sci
Asunto de la revista:
BIOQUIMICA
Año:
1996
Tipo del documento:
Article
País de afiliación:
Estados Unidos