1ot5 | pdb_00001ot5
The 2.4 Angstrom Crystal Sructure of Kex2 in complex with a peptidyl-boronic acid inhibitor
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Overview
This paper reports the first structure of a member of the Kex2/furin family of eukaryotic pro-protein processing proteases, which cleave sites consisting of pairs or clusters of basic residues. Reported is the 2.4 A resolution crystal structure of the two-domain protein ssKex2 in complex with an Ac-Ala-Lys-boroArg inhibitor (R = 20.9%, R(free) = 24.5%). The Kex2 proteolytic domain is similar in its global fold to the subtilisin-like superfamily of degradative proteases. Analysis of the complex provides a structural basis for the extreme selectivity of this enzyme family that has evolved from a nonspecific subtilisin-like ancestor. The P-domain of ssKex2 has a novel jelly roll like fold consisting of nine beta strands and may potentially be involved, along with the buried Ca(2+) ion, in creating the highly determined binding site for P(1) arginine.
About this Structure
1OT5 is a Single protein structure of sequence from Saccharomyces cerevisiae with NAG, CA and ACE as ligands. Active as Kexin, with EC number 3.4.21.61 Full crystallographic information is available from OCA.
Reference
2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor., Holyoak T, Wilson MA, Fenn TD, Kettner CA, Petsko GA, Fuller RS, Ringe D, Biochemistry. 2003 Jun 10;42(22):6709-18. PMID:12779325
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