Literature DB >> 22884395

Allosteric post-translational modification codes.

Ruth Nussinov1, Chung-Jung Tsai, Fuxiao Xin, Predrag Radivojac.   

Abstract

Post-translational modifications (PTMs) have been recognized to impact protein function in two ways: (i) orthosterically, via direct recognition by protein domains or through interference with binding; and (ii) allosterically, via conformational changes induced at the functional sites. Because different chemical types of PTMs elicit different structural alterations, the effects of combinatorial codes of PTMs are vastly larger than previously believed. Combined with orthosteric PTMs, the impact of PTMs on cellular regulation is immense. From an evolutionary standpoint, harnessing this immense, yet highly specific, PTM code is an extremely efficient vehicle that can save a cell several-fold in gene number and speed up its response to environmental change.
Copyright © 2012 Elsevier Ltd. All rights reserved.

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Year:  2012        PMID: 22884395     DOI: 10.1016/j.tibs.2012.07.001

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  71 in total

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8.  Linking post-translational modifications and variation of phenotypic traits.

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Journal:  Mol Cell Proteomics       Date:  2012-12-27       Impact factor: 5.911

9.  Allosteric Control of a Plant Receptor Kinase through S-Glutathionylation.

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10.  The Mechanism of ATP-Dependent Allosteric Protection of Akt Kinase Phosphorylation.

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