NDLI: Specificity and reactive loop length requirements for crmA inhibition of serine proteases

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Specificity and reactive loop length requirements for crmA inhibition of serine proteases

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Tesch, Lisa D. Raghavendra, Manikanahally P. Olson, Steven T. Bedsted-Faarvang, Tina Gettins, Peter G. W.
Description	Country affiliation: United States Author Affiliation: Tesch LD ( Center for Molecular Biology of Oral Diseases, College of Dentistry, University of Illinois at Chicago, Chicago, IL 60612, USA.)
Abstract	The viral serpin, crmA, is distinguished by its small size and ability to inhibit both serine and cysteine proteases utilizing a reactive loop shorter than most other serpins. Here, we characterize the mechanism of crmA inhibition of serine proteases and probe the reactive loop length requirements for inhibition with two crmA reactive loop variants. P1 Arg crmA inhibited the trypsin-like proteases, thrombin, and factor Xa, with moderate efficiencies (approximately 10(2)-10(4) M(-1)sec(-1)), near equimolar inhibition stoichiometries, and formation of SDS-stable complexes which were resistant to dissociation (k(diss) approximately 10(-7) sec(-1)), consistent with a serpin-type inhibition mechanism. Trypsin was not inhibited, but efficiently cleaved the variant crmA as a substrate (k(cat)/K(M) of approximately 10(6) M(-1) sec(-1)). N-terminal sequencing confirmed that the P1 Arg-P1'Cys bond was the site of cleavage. Altering the placement of the Arg in a double mutant P1 Gly-P1'Arg crmA resulted in minimal ability to inhibit any of the trypsin family proteases. This variant was cleaved by the proteases approximately 10-fold less efficiently than P1 Arg crmA. Surprisingly, pancreatic elastase was rapidly inhibited by wild-type and P1 Arg crmAs (10(5)-10(6) M(-1)sec(-1)), although with elevated inhibition stoichiometries and higher rates of complex dissociation. N-terminal sequencing showed that elastase attacked the P1'Cys-P2'Ala bond, indicating that crmA can inhibit proteases using a reactive loop length similar to that used by other serpins, but with variations in this inhibition arising from different effective P2 residues. These results indicate that crmA inhibits serine proteases by the established serpin conformational trapping mechanism, but is unusual in inhibiting through either of two adjacent reactive sites.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	2
Volume Number	14
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2005-02-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Serine Endopeptidases Chemistry Serine Proteinase Inhibitors Serpins Viral Proteins Antithrombins Arginine Binding Sites Chromatography Cysteine Dose-response Relationship, Drug Electrophoresis, Polyacrylamide Gel Enzyme Inhibitors Pharmacology Escherichia Coli Metabolism Factor Xa Kinetics Mutagenesis Pancreatic Elastase Peptide Hydrolases Protein Binding Protein Conformation Protein Folding Protein Structure, Tertiary Serine Time Factors Trypsin Research Support, N.i.h., Extramural Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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