Annals of the New York Academy of Sciences (2012). Pages: 1-6. Charalampos G Kalodimos et al.
Allostery is a fundamental process by which distant sites within a protein system sense each other. Allosteric regulation is such an efficient mechanism that it is used to control protein activity in most biological processes, including signal transduction, metabolism, catalysis, and gene regulation. Over recent years, our view and understanding of the fundamental principles underlying allostery have been enriched and often utterly reshaped. This has been especially so for powerful techniques such as nuclear magnetic resonance spectroscopy, which offers an atomic view of the intrinsic motions of proteins. Here, I discuss recent results on the catabolite activator protein (CAP) that have drastically revised our view about how allosteric interactions are modulated. CAP has provided the first experimentally identified system showing that (i) allostery can be mediated through changes in protein motions, in the absence of changes in the mean structure of the protein, and (ii) favorable changes in protein motions may activate allosteric proteins that are otherwise structurally inactive.
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Mapping allostery through the covariance analysis of NMR chemical shifts [Biophysics and Computational Biology]
Mapping allostery through the covariance analysis of NMR chemical shifts
Selvaratnam, R., Chowdhury, S., VanSchouwen, B., Melacini, G....
Date: 2011-04-12
Allostery is a fundamental mechanism of regulation in biology. The residues at the end points of long-range allosteric perturbations are commonly identified by the comparative analyses of structures and dynamics in apo and effector-bound states. However, the networks of interactions mediating the propagation of allosteric signals between the end points often remain elusive. Here we show that the covariance analysis of NMR chemical...
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04-13-2011 01:15 AM
Mapping allostery through the covariance analysis of NMR chemical shifts.
Mapping allostery through the covariance analysis of NMR chemical shifts.
Mapping allostery through the covariance analysis of NMR chemical shifts.
Proc Natl Acad Sci U S A. 2011 Mar 28;
Authors: Selvaratnam R, Chowdhury S, Vanschouwen B, Melacini G
Allostery is a fundamental mechanism of regulation in biology. The residues at the end points of long-range allosteric perturbations are commonly identified by the comparative analyses of structures and dynamics in apo and effector-bound states. However, the networks of interactions mediating the...
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03-31-2011 06:24 PM
[MWClarkson blog] Dynamic origins of PBX1 homeodomain allostery
Dynamic origins of PBX1 homeodomain allostery
http://www.researchblogging.org/public/citation_icons/rb2_large_gray.pngIn the Monod-Wyman-Changeux model for cooperative binding, proteins exist in an equilibrium of low-affinity and high-affinity states in solution, absent any ligand. In this view, although it may appear that the binding of a ligand causes a conformational transition, it actually stabilizes one conformation from a pre-existing equilibrium. In the past several years, advanced NMR techniques have yielded increasing evidence that these structural equilibria exist for a number of...
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12-02-2010 08:41 AM
Protein dynamics and allostery: an NMR view.
Protein dynamics and allostery: an NMR view.
Related Articles Protein dynamics and allostery: an NMR view.
Curr Opin Struct Biol. 2010 Nov 23;
Authors: Tzeng SR, Kalodimos CG
Allostery, the process by which distant sites within a protein system are energetically coupled, is an efficient and ubiquitous mechanism for activity regulation. A purely mechanical view of allostery invoking only structural changes has developed over the decades as the classical view of the phenomenon. However, a fast growing list of examples illustrate the intimate link...
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11-27-2010 02:45 PM
[NMR paper] Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Related Articles Dynamic activation of protein function: a view emerging from NMR spectroscopy.
Nat Struct Biol. 2001 Nov;8(11):926-31
Authors: Wand AJ
Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Particular emphasis is placed on the potential of fast side chain motion...
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11-19-2010 08:44 PM
[NMR paper] Using NMR as a probe of protein structure and function.
Using NMR as a probe of protein structure and function.
Related Articles Using NMR as a probe of protein structure and function.
Biochem Soc Trans. 1999 Aug;27(4):701-13
Authors: Malthouse JP
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11-18-2010 08:31 PM
[NMR paper] Relationship between electrostatics and redox function in human thioredoxin: characte
Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR.
Related Articles Relationship between electrostatics and redox function in human thioredoxin: characterization of pH titration shifts using two-dimensional homo- and heteronuclear NMR.
Biochemistry. 1992 Apr 7;31(13):3442-52
Authors: Forman-Kay JD, Clore GM, Gronenborn AM
The electrostatic behavior of potentially titrating groups in reduced human thioredoxin was investigated...
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08-21-2010 11:41 PM
Finding protein function from its NMR structure
For proteomics folks who gamble with their careers by promising discovery of protein function from NMR structures that may not look like any known proteins.
Find the best structural matches in a protein database
DALI
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Align structure of your protein with several proteins of your interest
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Protein function and allostery: a dynamic relationship.
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