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A conserved helix‐unfolding motif in the naturally unfolded proteins
Author(s) -
Zetina Carlos R.
Publication year - 2001
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.1113
Subject(s) - motif (music) , structural motif , unfolded protein response , chemistry , protein folding , sequence motif , protein secondary structure , crystallography , biology , computational biology , biochemistry , dna , physics , endoplasmic reticulum , acoustics
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.