Crystallography of serpins and serpin complexes

Research output: Chapter in Book/Report/Conference proceedingChapter (Book)Researchpeer-review

12 Citations (Scopus)

Abstract

The serpin superfamily of protease inhibitors undergoes a remarkable conformational change to inhibit target proteases. To date, over 80 different serpin crystal structures have been determined. These data reveal that the serpin monomer can adopt five different conformations (native, partially inserted native, delta-form, latent, and cleaved). Further, recent studies have also revealed that serpins can domain swap; biochemical data suggest such an event underlies serpin polymerization in diseases such as antitrypsin deficiency. Here, we provide a comprehensive analysis on crystallization of serpins in context of the structural landscape of the serpin superfamily.
Original languageEnglish
Title of host publicationMethods in Enzymology, Volume 501: Serpin Structure and Evolution
EditorsJames C Whisstock, Phillip I Bird
Place of PublicationUSA
PublisherAcademic Press
Pages63 - 87
Number of pages25
ISBN (Print)9780123859501
DOIs
Publication statusPublished - 2011

Cite this