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Conformational flexibility may explain multiple cellular roles of PEST motifs
Author(s) -
Sandhu Kuljeet Singh,
Dash Debasis
Publication year - 2006
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.20918
Subject(s) - dihedral angle , protein data bank (rcsb pdb) , flexibility (engineering) , protein data bank , pest analysis , protein structure , computational biology , biology , bioinformatics , chemistry , biochemistry , mathematics , botany , organic chemistry , molecule , hydrogen bond , statistics
PEST sequences are one of the major motifs that serve as signal for the protein degradation and are also involved in various cellular processes such as phosphorylation and protein–protein interaction. In our earlier study, we found that these motifs contribute largely to eukaryotic protein disorder. This observation led us to evaluate their conformational variability in the nonredundant Protein Data Bank (PDB) structures. For this purpose, crystallographic temperature factors, structural alignment of multiple NMR models, and dihedral angle order parameters have been used in this study. The study has revealed the hypermobility of PEST motifs as compared to other regions of the protein. Conformational flexibility may allow them to participate in number of molecular interactions under different conditions. This analysis may explain the role of protein backbone flexibility in bringing about multiple cellular roles of PEST motifs. Proteins 2006. © 2006 Wiley‐Liss, Inc.