An overview of the serpin superfamily

Ruby HP Law¹, Qingwei Zhang¹^,2, Sheena McGowan¹^,2^,3, Ashley M Buckle¹^,2, Gary A Silverman⁴, Wilson Wong¹^,3, Carlos J Rosado¹^,3, Chris G Langendorf¹^,3, Rob N Pike¹, Philip I Bird¹ and James C Whisstock¹^,2^,4

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

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

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

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

author email corresponding author email

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


Published:	30 May 2006

Subject areas: Biochemistry and structural biology, Medicine, Genetics

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.