1btp
From Proteopedia
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UNIQUE BINDING OF A NOVEL SYNTHETIC INHIBITOR, N-[3-[4-[4-(AMIDINOPHENOXY)-CARBONYL]PHENYL]-2-METHYL-2-PROPENOYL]-N-ALLYLGLYCINE METHANESULFONATE TO BOVINE TRYPSIN, REVEALED BY THE CRYSTAL STRUCTURE OF THE COMPLEX
Overview
Trypsin and, N-[3-[4-[4-(amidinophenoxy)carbonyl]phenyl]-2-methyl-2-propenoyl]-, N-allylglycine methanesulfonate (1), a newly designed and orally active, synthetic trypsin inhibitor, were cocrystallized. The space group of the, crystal is P2(1)2(1)2(1) with cell constants a = 63.74 A, b = 63.08 A, and, c = 69.38 A, which is nearly identical to that of the orthorhombic crystal, of guanidinobenzoyltrypsin. The structure was refined to a, crystallographic residual R = 0.176. The refined model of the 1-trypsin, complex provides the structural basis for the reaction mechanism of 1. On, the basis of the present X-ray results, it is proposed that the potent, inhibitory activity of 1 is mainly due to the formation of an acylated, trypsin through an "inverse substrate mechanism" and its low rate of, deacylation.
About this Structure
1BTP is a Single protein structure of sequence from Bos taurus with CA as ligand. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
Unique binding of a novel synthetic inhibitor, N-[3-[4-[4-(amidinophenoxy)carbonyl]phenyl]-2-methyl-2-propenoyl]- N-allylglycine methanesulfonate, to bovine trypsin, revealed by the crystal structure of the complex., Odagaki Y, Nakai H, Senokuchi K, Kawamura M, Hamanaka N, Nakamura M, Tomoo K, Ishida T, Biochemistry. 1995 Oct 3;34(39):12849-53. PMID:7548040
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