Abstract
The serpin family comprises a structurally similar, yet functionally diverse, set of proteins. Named originally for their function as serine proteinase inhibitors, many of its members are not inhibitors but rather chaperones, involved in storage, transport, and other roles. Serpins are found in genomes of all kingdoms, with 36 human protein-coding genes and five pseudogenes. The mouse has 60 Serpin functional genes, many of which are orthologous to human SERPIN genes and some of which have expanded into multiple paralogous genes. Serpins are found in tissues throughout the body; whereas most are extracellular, there is a class of intracellular serpins. Serpins appear to have roles in inflammation, immune function, tumorigenesis, blood clotting, dementia, and cancer metastasis. Further characterization of these proteins will likely reveal potential biomarkers and therapeutic targets for disease.
Highlights
Serpins represent the largest and most functionally diverse family of protease inhibitors
Serpins have well-conserved secondary structures with an exposed reactive center loop (RCL) (Figure 1), which interacts with the protease active site to inhibit protease activity [5]
Serpins are a large class of diverse proteins, which contribute to numerous physiological and pathological conditions
Summary
Serpins represent the largest and most functionally diverse family of protease inhibitors. Serpins have well-conserved secondary structures with an exposed reactive center loop (RCL) (Figure 1), which interacts with the protease active site to inhibit protease activity [5]. Structure function Serpins have a metastable structure that is required for their function It consists of a highly conserved secondary structure with three β-sheets (A, B, and C), nine α-helices and a RCL (Figure 1), which serve as bait for target proteases [4,6]. Well-conserved throughout the serpin family, the tertiary structure of scaffold allows for a conformational change critical to protease inhibitor activity [4]. In their native state, serpins exist as monomeric proteins. The polymeric form has a loop sheet mechanism whereby the RCL that would be inserted into the same serpin is
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
