1BTY

Crystal structure of beta-trypsin in complex with benzamidine

Summary for 1BTY

• Entry DOI: 10.2210/pdb1bty/pdb
• Descriptor: BETA-TRYPSIN, CALCIUM ION, BENZAMIDINE, ... (4 entities in total)
• Functional Keywords: benzamidine inhibited, hydrolase (serine proteinase), hydrolase
• Biological source: Bos taurus (BOVINE)
• Cellular location: Secreted, extracellular space: P00760
• Total number of polymer chains: 1
• Total formula weight: 24173.18

Authors

Stroud, R.M.,Katz, B.A.,Finer-Moore, J. (deposition date: 1995-05-17, release date: 1995-10-15, Last modification date: 2024-11-13)

Primary citation

Katz, B.A.,Finer-Moore, J.,Mortezaei, R.,Rich, D.H.,Stroud, R.M.
Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface.
Biochemistry, 34:8264-8280, 1995

PubMed Abstract: A novel class of mechanism-based inhibitors of the serine proteases is developed using epitaxial selection. Tripeptide boronates esterified by an alcohol or alcohols at the boron retain the tight binding to trypsin-like enzymes associated with transition-state analogs and incorporate additional groups that can be utilized for selectivity between proteases. Formed by reaction of a series of alcohols with the inhibitor boronate oxygen(s), the most structurally compatible alcohol-derivatized inhibitors are either selected by binding to the enzyme (epitaxial selection) or assembled by epitaxial reaction on the enzyme surface. Mass spectrometry of the derivatized boronates and X-ray crystallography of the complexes identify the chemical structures and the three-dimensional interactions of inhibitors generated. This scheme also engineers novel, potent (Ki approximately 7 nM), and more specific inhibitors of individual serine proteases, by derivitizations of compounds obtained by epitaxial selection.

PubMed: 7599119
DOI: 10.1021/bi00026a008

Experimental method

X-RAY DIFFRACTION (1.5 Å)