Serpin crystal structure and serpin polymer structure.
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.
Marszal
Ewa
E
Division of Hematology, Office of Blood Research and Review, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892, USA. ewa.marszal@fda.hhs.gov
Shrake
Andrew
A
D000595:Amino Acid Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D009154:Mutation; D011108:Polymers / Q000737:chemistry; D011487:Protein Conformation; D015843:Serpins / Q000737:chemistry* / Q000648:ultrastructure*
D046912:Multiprotein Complexes; D011108:Polymers; D015843:Serpins