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Statements

Subject Item
n2:RIV%2F67179843%3A_____%2F10%3A00359496%21RIV12-AV0-67179843
rdf:type
skos:Concept n19:Vysledek
dcterms:description
A controversial prediction of the famous allostery model of Monod, Wyman, and Changeux is that constraints imposed on protein subunits by multimerization are relaxed by ligand binding, but with conservation of symmetry in partially-liganded states. Interpretation of thermodynamic ligand-binding data through the lens of molecular dynamics simulation has led to structural and energetic description of such a state for the hexameric Escherichia coli arginine repressor, which displays strong negative cooperativity of L-arginine binding. The results indicate that partially-liganded states can be structurally symmetric despite their conceptual asymmetry. The symmetric relaxed state is visualized as a multimer with all subunits anchored near the center, and with motions transferred to the periphery of the assembly. Thus, even during sequential filling of binding sites, symmetry can be maintained by exploiting the dynamics of the assembly and the distributed nature of its cohesive free energy. A controversial prediction of the famous allostery model of Monod, Wyman, and Changeux is that constraints imposed on protein subunits by multimerization are relaxed by ligand binding, but with conservation of symmetry in partially-liganded states. Interpretation of thermodynamic ligand-binding data through the lens of molecular dynamics simulation has led to structural and energetic description of such a state for the hexameric Escherichia coli arginine repressor, which displays strong negative cooperativity of L-arginine binding. The results indicate that partially-liganded states can be structurally symmetric despite their conceptual asymmetry. The symmetric relaxed state is visualized as a multimer with all subunits anchored near the center, and with motions transferred to the periphery of the assembly. Thus, even during sequential filling of binding sites, symmetry can be maintained by exploiting the dynamics of the assembly and the distributed nature of its cohesive free energy.
dcterms:title
Symmetric Allosteric Mechanism of Hexameric Escherichia coli Arginine Repressor Exploits Competition between L-Arginine Ligands and Resident Arginine Residues Symmetric Allosteric Mechanism of Hexameric Escherichia coli Arginine Repressor Exploits Competition between L-Arginine Ligands and Resident Arginine Residues
skos:prefLabel
Symmetric Allosteric Mechanism of Hexameric Escherichia coli Arginine Repressor Exploits Competition between L-Arginine Ligands and Resident Arginine Residues Symmetric Allosteric Mechanism of Hexameric Escherichia coli Arginine Repressor Exploits Competition between L-Arginine Ligands and Resident Arginine Residues
skos:notation
RIV/67179843:_____/10:00359496!RIV12-AV0-67179843
n3:aktivita
n5:Z n5:S n5:P n5:I
n3:aktivity
I, P(GAP207/10/1934), P(LC06010), S, Z(AV0Z60870520)
n3:cisloPeriodika
6
n3:dodaniDat
n8:2012
n3:domaciTvurceVysledku
n16:2486024 n16:6326633
n3:druhVysledku
n13:J
n3:duvernostUdaju
n9:S
n3:entitaPredkladatele
n4:predkladatel
n3:idSjednocenehoVysledku
291364
n3:idVysledku
RIV/67179843:_____/10:00359496
n3:jazykVysledku
n17:eng
n3:klicovaSlova
molecular-dynamics simulations; free-energy calculations; structural basis; DNA-binding domain; bacillus-stearothermophilus; T4 lysozyme; proteins; hemoglobin; model; affinity
n3:klicoveSlovo
n10:molecular-dynamics%20simulations n10:proteins n10:T4%20lysozyme n10:affinity n10:model n10:bacillus-stearothermophilus n10:hemoglobin n10:free-energy%20calculations n10:DNA-binding%20domain n10:structural%20basis
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[D2A97D0FFBDC]
n3:nazevZdroje
PLoS Computational Biology
n3:obor
n18:EH
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
6
n3:projekt
n14:GAP207%2F10%2F1934 n14:LC06010
n3:rokUplatneniVysledku
n8:2010
n3:svazekPeriodika
6
n3:tvurceVysledku
Carey, J. Strawn, R. Ettrich, Rüdiger Melicherčík, Milan Stockner, T. Green, M.
n3:wos
000279341000007
n3:zamer
n12:AV0Z60870520
s:issn
1553-734X
s:numberOfPages
12
n15:doi
10.1371/journal.pcbi.1000801