Literature DB >> 18353365

Allostery: absence of a change in shape does not imply that allostery is not at play.

Chung-Jung Tsai1, Antonio del Sol, Ruth Nussinov.   

Abstract

Allostery is essential for controlled catalysis, signal transmission, receptor trafficking, turning genes on and off, and apoptosis. It governs the organism's response to environmental and metabolic cues, dictating transient partner interactions in the cellular network. Textbooks taught us that allostery is a change of shape at one site on the protein surface brought about by ligand binding to another. For several years, it has been broadly accepted that the change of shape is not induced; rather, it is observed simply because a larger protein population presents it. Current data indicate that while side chains can reorient and rewire, allostery may not even involve a change of (backbone) shape. Assuming that the enthalpy change does not reverse the free-energy change due to the change in entropy, entropy is mainly responsible for binding.

Mesh:

Year:  2008        PMID: 18353365      PMCID: PMC2684958          DOI: 10.1016/j.jmb.2008.02.034

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  53 in total

1.  Order changes within receptor systems upon ligand binding: receptor tightening/oligomerisation and the interpretation of binding parameters.

Authors:  Dudley H Williams; Dominic P O'Brien; Alan M Sandercock; Elaine Stephens
Journal:  J Mol Biol       Date:  2004-07-02       Impact factor: 5.469

2.  Use of binding enthalpy to drive an allosteric transition.

Authors:  Patrick H Brown; Dorothy Beckett
Journal:  Biochemistry       Date:  2005-03-01       Impact factor: 3.162

Review 3.  Probing the binding entropy of ligand-protein interactions by NMR.

Authors:  Steve W Homans
Journal:  Chembiochem       Date:  2005-09       Impact factor: 3.164

4.  Dynamic allostery of protein alpha helical coiled-coils.

Authors:  Rhoda J Hawkins; Tom C B McLeish
Journal:  J R Soc Interface       Date:  2006-02-22       Impact factor: 4.118

Review 5.  The lactose repressor system: paradigms for regulation, allosteric behavior and protein folding.

Authors:  C J Wilson; H Zhan; L Swint-Kruse; K S Matthews
Journal:  Cell Mol Life Sci       Date:  2007-01       Impact factor: 9.261

6.  Propagation of dynamic changes in barnase upon binding of barstar: an NMR and computational study.

Authors:  Anastasia Zhuravleva; Dmitry M Korzhnev; Svetlana B Nolde; Lewis E Kay; Alexander S Arseniev; Martin Billeter; Vladislav Yu Orekhov
Journal:  J Mol Biol       Date:  2007-01-24       Impact factor: 5.469

7.  Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase.

Authors:  Luc Fetler; Evan R Kantrowitz; Patrice Vachette
Journal:  Proc Natl Acad Sci U S A       Date:  2007-01-03       Impact factor: 11.205

8.  Evaluation of energetic and dynamic coupling networks in a PDZ domain protein.

Authors:  Ernesto J Fuentes; Steven A Gilmore; Randall V Mauldin; Andrew L Lee
Journal:  J Mol Biol       Date:  2006-09-01       Impact factor: 5.469

9.  Calorimetric studies of the energetics of protein-DNA interactions in the E. coli methionine repressor (MetJ) system.

Authors:  A Cooper; A McAlpine; P G Stockley
Journal:  FEBS Lett       Date:  1994-07-04       Impact factor: 4.124

10.  Configurational entropy and cooperativity between ligand binding and dimerization in glycopeptide antibiotics.

Authors:  Sutjano Jusuf; Patrick J Loll; Paul H Axelsen
Journal:  J Am Chem Soc       Date:  2003-04-02       Impact factor: 15.419

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  198 in total

Review 1.  Allosteric regulation of protease activity by small molecules.

Authors:  Aimee Shen
Journal:  Mol Biosyst       Date:  2010-06-10

Review 2.  Metalloregulatory proteins: metal selectivity and allosteric switching.

Authors:  Hermes Reyes-Caballero; Gregory C Campanello; David P Giedroc
Journal:  Biophys Chem       Date:  2011-04-05       Impact factor: 2.352

3.  Dynamical allosterism in the mechanism of action of DNA mismatch repair protein MutS.

Authors:  Susan N Pieniazek; Manju M Hingorani; D L Beveridge
Journal:  Biophys J       Date:  2011-10-05       Impact factor: 4.033

Review 4.  On the expanding terminology in the GPCR field: the meaning of receptor mosaics and receptor heteromers.

Authors:  Luigi F Agnati; Diego Guidolin; Jean Pierre Vilardaga; Francisco Ciruela; Kjell Fuxe
Journal:  J Recept Signal Transduct Res       Date:  2010-10       Impact factor: 2.092

5.  Substrate-modulated thermal fluctuations affect long-range allosteric signaling in protein homodimers: exemplified in CAP.

Authors:  Hedvika Toncrova; Tom C B McLeish
Journal:  Biophys J       Date:  2010-05-19       Impact factor: 4.033

6.  Entropic mechanism of large fluctuation in allosteric transition.

Authors:  Kazuhito Itoh; Masaki Sasai
Journal:  Proc Natl Acad Sci U S A       Date:  2010-04-12       Impact factor: 11.205

7.  Use of allostery to identify inhibitors of calmodulin-induced activation of Bacillus anthracis edema factor.

Authors:  Elodie Laine; Christophe Goncalves; Johanna C Karst; Aurélien Lesnard; Sylvain Rault; Wei-Jen Tang; Thérèse E Malliavin; Daniel Ladant; Arnaud Blondel
Journal:  Proc Natl Acad Sci U S A       Date:  2010-06-07       Impact factor: 11.205

8.  Interaction energy based protein structure networks.

Authors:  M S Vijayabaskar; Saraswathi Vishveshwara
Journal:  Biophys J       Date:  2010-12-01       Impact factor: 4.033

9.  Allosteric Dynamic Control of Binding.

Authors:  Fidan Sumbul; Saliha Ece Acuner-Ozbabacan; Turkan Haliloglu
Journal:  Biophys J       Date:  2015-08-31       Impact factor: 4.033

10.  Dynamically Coupled Residues within the SH2 Domain of FYN Are Key to Unlocking Its Activity.

Authors:  Radu Huculeci; Elisa Cilia; Agatha Lyczek; Lieven Buts; Klaartje Houben; Markus A Seeliger; Nico van Nuland; Tom Lenaerts
Journal:  Structure       Date:  2016-09-29       Impact factor: 5.006

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