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Curr Opin Struct Biol. 2006 Dec;16(6):761-8. Epub 2006 Oct 31.

Molecular gymnastics: serpin structure, folding and misfolding.

Author information

1
Protein Crystallography Unit, Department of Biochemistry and Molecular Biology, Clayton Campus, Melbourne 3800, Australia. james.whisstock@med.monash.edu.au

Abstract

The native state of serpins represents a long-lived intermediate or metastable structure on the serpin folding pathway. Upon interaction with a protease, the serpin trap is sprung and the molecule continues to fold into a more stable conformation. However, thermodynamic stability can also be achieved through alternative, unproductive folding pathways that result in the formation of inactive conformations. Our increasing understanding of the mechanism of protease inhibition and the dynamics of native serpin structures has begun to reveal how evolution has harnessed the actual process of protein folding (rather than the final folded outcome) to elegantly achieve function. The cost of using metastability for function, however, is an increased propensity for misfolding.

PMID:
17079131
DOI:
10.1016/j.sbi.2006.10.005
[Indexed for MEDLINE]

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