Serpin crystal structure and serpin polymer structure

Arch Biochem Biophys. 2006 Sep 1;453(1):123-9. doi: 10.1016/j.abb.2006.03.006. Epub 2006 Mar 23.

Abstract

Serpins are a family of structurally homologous proteins having metastable native structures. As a result, a serpin variant destabilized by mutation(s) has a tendency to undergo conformational changes leading to inactive forms, e.g., the latent form and polymer. Serpin polymers are involved in a number of conformational diseases. Although several models for polymer structure have been proposed, the actual structure remains unknown. Here, we provide a comprehensive list of serpins, both free and in complexes, deposited in the Protein Data Bank. Our discussion focuses on structures that potentially can contribute to a better understanding of polymer structure.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Models, Molecular*
  • Molecular Sequence Data
  • Multiprotein Complexes / chemistry
  • Multiprotein Complexes / ultrastructure
  • Mutation
  • Polymers / chemistry
  • Protein Conformation
  • Serpins / chemistry*
  • Serpins / ultrastructure*

Substances

  • Multiprotein Complexes
  • Polymers
  • Serpins