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- Publisher
- Wiley
- Copyright
- Copyright © 2001 Wiley Subscription Services
- ISSN
- 0887-3585
- eISSN
- 1097-0134
- DOI
- 10.1002/prot.1113
- Publisher site
- See Article on Publisher Site
Abstract
Among the naturally unfolded proteins there are many polypeptides that retain an extended conformation in the absence of any apparent signal. Using sequence alignment and secondary structure prediction tools, a conserved (LS/SL)(D/E)(D/E)(D/E)X(E/D) motif is uncovered in the vicinity of the N‐terminus of their unfolded helices. A comparison of these data with published observations allows one to propose that the (LS/SL)(D/E)(D/E)(D/E)X(E/D) motif is a helix‐unfolding signal. Furthermore, the strong similarity between this motif and the STXXDE casein kinase II phosphorylation site suggests a regulatory mechanism for the naturally unfolded proteins within the cell. Proteins 2001;44:479–483. © 2001 Wiley‐Liss, Inc.
Journal
Proteins: Structure Function and Bioinformatics – Wiley
Published: Jan 1, 2001
Keywords: ; ; ; ;