Highly Accessed Review

An overview of the serpin superfamily

Ruby HP Law1, Qingwei Zhang12, Sheena McGowan123, Ashley M Buckle12, Gary A Silverman4, Wilson Wong13, Carlos J Rosado13, Chris G Langendorf13, Rob N Pike1, Philip I Bird1 and James C Whisstock124*

Author affiliations

1 Department of Biochemistry and Molecular Biology, Monash University, Clayton Campus, Melbourne VIC 3800, Australia

2 Victorian Bioinformatics Consortium, Monash University, Clayton Campus, Melbourne VIC 3800, Australia

3 ARC Centre for Structural and Functional Microbial Genomics, Monash University, Clayton Campus, Melbourne VIC 3800, Australia

4 Magee-Womens Research Institute, Children's Hospital of Pittsburgh, Department of Pediatrics, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213, USA

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Citation and License

Genome Biology 2006, 7:216  doi:10.1186/gb-2006-7-5-216

Published: 30 May 2006

Abstract

Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades, including the mammalian coagulation pathways. Serpins are conformationally labile and many of the disease-linked mutations of serpins result in misfolding or in pathogenic, inactive polymers.