title: Crystallography of serpins and serpin complexes.
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, δ-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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria, Australia.
authors.forename: M A
authors.initials: MA
authors.lastname: Dunstone
authors.forename: James C
authors.initials: JC
authors.lastname: Whisstock
mesh_terms: D000818:Animals; D000990:Antithrombin III / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification*; D016466:CHO Cells; D002645:Chickens; D006224:Cricetinae; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D004926:Escherichia coli; D057809:HEK293 Cells; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D008967:Molecular Biology / Q000379:methods*; D017395:Plasminogen Activator Inhibitor 1 / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification*; D058105:Polymerization; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification*; D000515:alpha 1-Antitrypsin / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification*
chemical_list: D017395:Plasminogen Activator Inhibitor 1; D011993:Recombinant Fusion Proteins; C051321:SERPINE1 protein, human; D000515:alpha 1-Antitrypsin; D000990:Antithrombin III