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EMBO reports 5, 11, 1046–1052 (2004)
doi:10.1038/sj.embor.7400276
Natively unfolded domains in endocytosis: hooks, lines and linkers
Timothy R. Dafforn1 & Corinne J. I. Smith2
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1 Department of Biosciences, University of Birmingham, Birmingham B15 2TT, UK
2 Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK
To whom correspondence should be addressed
Corinne J. I. Smith Tel: +44 24 76 52 2 461; Fax: +44 024 76 52 3 568; corinne.smith@warwick.ac.uk
Received 14 June 2004; Accepted 15 September 2004.
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Abstract
It is commonly assumed that a protein must adopt a tertiary structure to achieve its active native state and that regions of a protein that are devoid of  -helix or  -sheet structures are functionally inert. Although extended proline-rich regions are recognized as presenting binding motifs to, for example, Src homology 2 (SH2) and SH3 domains, the idea persists that natively unfolded regions in functional proteins are simply 'spacers' between the folded domains. Such a view has been challenged in recent years and the importance of natively unfolded proteins in biology is now being recognized. In this review, we highlight the role of natively unfolded domains in the field of endocytosis, and show that some important endocytic proteins lack a traditionally folded structure and harbour important binding motifs in their unstructured linker regions.
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