Molecular Modeling of the Substrate Specificity of Prohormone Convertases SPC2 and SPC3∗
G Lipkind, Q Gong, DF Steiner - Journal of Biological Chemistry, 1995 - ASBMB
In this paper we describe the results of molecular modeling of the structures of the active
sites of two subtilisin-like prohormone convertases (SPCs), SPC2 (PC2) and SPC3
(PC1/PC3). These enzymes are members of a recently discovered family of cellular
proteases involved in the processing of precursor proteins. Although these proteases all
possess catalytic domains similar to the bacterial subtilisins no tertiary structural data from x-
ray analysis are yet available. We have shown that despite the high structural homology of …
sites of two subtilisin-like prohormone convertases (SPCs), SPC2 (PC2) and SPC3
(PC1/PC3). These enzymes are members of a recently discovered family of cellular
proteases involved in the processing of precursor proteins. Although these proteases all
possess catalytic domains similar to the bacterial subtilisins no tertiary structural data from x-
ray analysis are yet available. We have shown that despite the high structural homology of …
