Journal
PROTEINS-STRUCTURE FUNCTION AND GENETICS
Volume 44, Issue 4, Pages 479-483Publisher
WILEY-LISS
DOI: 10.1002/prot.1113
Keywords
unfolded helix; conserved signature; unfolding activity; naturally unstructured proteins; reversible phosphorylation
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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. (C) 2001 Wiley-Liss, Inc.
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