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.
|Title of host publication||Methods in Enzymology, Volume 501: Serpin Structure and Evolution|
|Editors||James C Whisstock, Phillip I Bird|
|Place of Publication||USA|
|Pages||63 - 87|
|Number of pages||25|
|Publication status||Published - 2011|