A conserved helix‐unfolding motif in the naturally unfolded proteins | Zendy

Zetina Carlos R. | Zendy

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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.

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