Related ArticlesStructural insights into the calcium-mediated allosteric transition in the C-terminal domain of calmodulin from NMR measurements.
Biochemistry. 2015 Nov 30;
Authors: Kukic P, Lundström P, Camilloni C, Evenäs J, Akke M, Vendruscolo M
Abstract
Calmodulin is a two-domain signalling protein that becomes activated upon binding cooperatively two pairs of calcium ions, leading to large-scale conformational changes that expose its binding site. Despite significant advances in understanding the structural biology of calmodulin function, the mechanistic details of the conformational transition between closed and open states have remained unclear. To investigate this transition, we used a combination of molecular dynamics simulations and NMR experiments on the Ca2+-saturated E140Q C-terminal domain variant. Using chemical shift restraints in replica-averaged metadynamics simulations, we obtained a high-resolution structural ensemble consisting of two conformational states, and validated such ensemble against three independent experimental datasets, namely inter-proton NOEs, 15N order parameters, and chemical shift differences between the exchanging states. Through a detailed analysis of this structural ensemble and of the corresponding statistical weights, we characterised a calcium-mediated conformational transition whereby the coordination of Ca2+ by just one oxygen of the bidentate ligand E140 triggers a concerted movement of the two EF-hands that exposes the target-binding site. This analysis provides atomistic insights into a possible Ca2+-mediated activation mechanism of calmodulin not achievable from static structures alone or from ensemble NMR measurements of the transition between conformations.
PMID: 26618792 [PubMed - as supplied by publisher]
[NMR paper] New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization.
New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization.
New insights into the role of the disordered WIP N-terminal domain revealed by NMR structural characterization.
FEBS J. 2014 Dec 11;
Authors: Elazari-Shalom H, Shaked H, Esteban-Martin S, Salvatella X, Barda-Saad M, Chill JH
Abstract
WASp-interacting protein (WIP) is an intrinsically disordered 503-residue polypeptide with a key role in actin polymerization in activated T cells. Its interaction with actin is mediated...
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[NMR paper] Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Overproduction of the N-terminal Anticodon-binding Domain of the Non-discriminating Aspartyl-tRNA Synthetase from Helicobacter pylori for Crystallization and NMR Measurements.
Protein Expr Purif. 2013 Feb 27;
Authors: Fuengfuloy P, Chuawong P, Suebka S, Wattana-Amorn P, Williams C, Crump MP, Songsiriritthigul C
Abstract
Aminoacyl-tRNA synthetases (aaRSs) covalently...
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03-05-2013 03:25 PM
[NMR paper] Cations as Switches of Amyloid-Mediated Membrane Disruption Mechanisms: Calcium and IAPP.
Cations as Switches of Amyloid-Mediated Membrane Disruption Mechanisms: Calcium and IAPP.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif Related Articles Cations as Switches of Amyloid-Mediated Membrane Disruption Mechanisms: Calcium and IAPP.
Biophys J. 2013 Jan 8;104(1):173-84
Authors: Sciacca MF, Milardi D, Messina GM, Marletta G, Brender JR, Ramamoorthy A, La Rosa C
Abstract
Disruption of the integrity of the plasma membrane by amyloidogenic proteins is linked to the pathogenesis...
[NMR paper] Calmodulin discriminates between the two enantiomers of the receptor-operated calcium
Calmodulin discriminates between the two enantiomers of the receptor-operated calcium channel blocker SK&F 96365: a study using 1H-NMR and chiral HPLC.
Related Articles Calmodulin discriminates between the two enantiomers of the receptor-operated calcium channel blocker SK&F 96365: a study using 1H-NMR and chiral HPLC.
Chirality. 1990;2(4):229-32
Authors: Reid DG, MacLachlan LK, Robinson SP, Camilleri P, Dyke CA, Thorpe CJ
1H nuclear magnetic resonance at 360 MHz shows that SK&F 96365 (1-(beta--p-methoxyphenethyl)-1H- imidazole hydrochloride),...