Related ArticlesContrasting roles of dynamics in protein allostery: NMR and structural studies of CheY and the third PDZ domain from PSD-95.
Biophys Rev. 2015 Jun;7(2):217-226
Authors: Lee AL
Abstract
Allosteric regulation is a ubiquitous phenomenon exploited in biological processes to control cells in a myriad of ways. It is also of emerging interest in the design of functional proteins and therapeutics. Even though allostery was proposed over 50*years ago and has been studied intensively from a structural perspective, many key details of allosteric mechanisms remain mysterious. Over the last decade significant attention*has been paid to the "dynamic component" of allostery, as opposed to the analysis of rigid structures. Nuclear magnetic resonance spectroscopy and its ability to detect conformationally dynamic processes at atomic resolution have played an important role in expanding our understanding of allosteric mechanisms and opening up new questions. This article focuses on work that highlights how protein dynamics can factor into allosteric processes in distinct ways. Two cases are contrasted. The first considers the "traditionally allosteric" protein CheY, which undergoes a conformational change as a key element of its allostery. The second considers the more rarely observed "dynamic allostery" in a PDZ domain, in which allosteric behavior arises from changes in internal structural dynamics. Interestingly, the dynamic processes in these two contrasting examples occur on different timescales. In the case of the PDZ domain, subsequent experimental and computational work is reviewed to reveal a more complete picture of this interesting case of allostery.
NMR Structural Studies of the C-Domain of Tcb2, A Calcium Binding Protein from Tetrahymena Thermophila
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Publication date: 16 February 2016
Source:Biophysical Journal, Volume 110, Issue 3, Supplement 1</br>
Author(s): Adina M. Kilpatrick, C. Andrew Fowler, Theodore Gurrola, Jerry E. Honts</br>
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[NMR paper] Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling.
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Structure. 2014 May 14;
Authors: Rizzo AA, Suhanovsky MM, Baker ML, Fraser LC, Jones LM, Rempel DL, Gross ML, Chiu W, Alexandrescu AT, Teschke CM
Abstract
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific...
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Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling
Multiple Functional Roles of the Accessory I-Domain of Bacteriophage P22 Coat Protein Revealed by NMR Structure and CryoEM Modeling
Publication date: Available online 15 May 2014
Source:Structure</br>
Author(s): Alessandro*A. Rizzo , Margaret*M. Suhanovsky , Matthew*L. Baker , LaTasha*C.R. Fraser , Lisa*M. Jones , Don*L. Rempel , Michael*L. Gross , Wah Chiu , Andrei*T. Alexandrescu , Carolyn*M. Teschke</br>
Some capsid proteins built on the ubiquitous HK97-fold have accessory domains imparting specific functions. Bacteriophage P22 coat protein has a unique...
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Structural Dynamics Studies of Fatty Acid Binding Protein-4 by Solution NMR Spectroscopy
Structural Dynamics Studies of Fatty Acid Binding Protein-4 by Solution NMR Spectroscopy
Publication date: 28 January 2014
Source:Biophysical Journal, Volume 106, Issue 2, Supplement 1</br>
Author(s): Adedolapo Ojoawo , Choua Xiong , Kim N. Ha</br>
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Protein dynamics and allostery: an NMR view.
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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] NMR structural studies of domain 1 of receptor-associated protein.
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J Biomol NMR. 2004 Jul;29(3):271-9
Authors: Wu Y, Migliorini M, Walsh J, Yu P, Strickland DK, Wang YX
The 39 kDa receptor-associated protein (RAP) is an endoplasmic reticulum resident protein that binds tightly to the low-density lipoprotein receptor-related protein (LRP) as well as to other members of the low-density lipoprotein receptor superfamily. The association of RAP with LRP prevents...
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Biochemistry. 1992 Apr 28;31(16):4150-6
Authors: O'Hare P, Williams G
We have overproduced and purified the carboxy-terminal transactivation domain of Vmw65 (VP16) of herpes simplex virus, and studied potential folding of the domain by 1H NMR. Two species of the acidic domain were obtained from the...
Contrasting roles of dynamics in protein allostery: NMR and structural studies of CheY and the third PDZ domain from PSD-95.
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