The role of conformational change in serpin structure and function

Détails

ID Serval
serval:BIB_3469CE882317
Type
Article: article d'un périodique ou d'un magazine.
Sous-type
Synthèse (review): revue aussi complète que possible des connaissances sur un sujet, rédigée à partir de l'analyse exhaustive des travaux publiés.
Collection
Publications
Titre
The role of conformational change in serpin structure and function
Périodique
Bioessays
Auteur(s)
Gettins  P., Patston  P. A., Schapira  M.
ISSN
0265-9247 (Print)
Statut éditorial
Publié
Date de publication
07/1993
Volume
15
Numéro
7
Pages
461-7
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Review --- Old month value: Jul
Résumé
Serpins are members of a family of structurally related protein inhibitors of serine proteinases, with molecular masses between 40 and 100kDa. In contrast to other, simpler, proteinase inhibitors, they may interact with proteinases as inhibitors, as substrates, or as both. They undergo conformational interconversions upon complex formation with proteinase, upon binding of some members to heparin, upon proteolytic cleavage at the reactive center, and under mild denaturing conditions. These conformational changes appear to be critical in determining the properties of the serpin. The structures and stabilities of these various forms may differ significantly. Although the detailed structural changes required for inhibition of proteinase have yet to be worked out, it is clear that the serpin does undergo a major conformational change. This is in contrast to other, simpler, families of protein inhibitors of serine proteinases, which bind in a substrate-like or product-like manner. Proteolytic cleavage of the serpin can result in a much more stable protein with new biological properties such as chemo-attractant behaviour. These structural transformations in serpins provide opportunities for regulation of the activity and properties of the inhibitor and are likely be important in vivo, where serpins are involved in blood coagulation, fibrinolysis, complement activation and inflammation.
Mots-clé
Amino Acid Sequence Binding Sites Heparin/chemistry Humans Models, Molecular Molecular Sequence Data Multigene Family Protein Binding *Protein Conformation Sequence Alignment Sequence Homology, Amino Acid Serine Endopeptidases/chemistry Serine Proteinase Inhibitors/*chemistry/physiology Structure-Activity Relationship
Pubmed
Web of science
Création de la notice
25/01/2008 16:28
Dernière modification de la notice
20/08/2019 14:21
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