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dc.contributor.authorLian, Lu-Yun
dc.contributor.authorPandalaneni, Sravan R.
dc.contributor.authorPatel, Pryank
dc.contributor.authorMcCue, Hannah V.
dc.contributor.authorHaynes, Lee P.
dc.contributor.authorBurgoyne, Robert D.
dc.date.accessioned2016-03-16T10:14:59Z
dc.date.available2016-03-16T10:14:59Z
dc.date.issued2011-11-16
dc.identifier.citationLian , L-Y , Pandalaneni , S R , Patel , P , McCue , H V , Haynes , L P & Burgoyne , R D 2011 , ' Characterisation of the interaction of the C-terminus of the dopamine D2 receptor with neuronal calcium sensor-1 ' , PLoS ONE , vol. 6 , no. 11 , pp. e27779 . https://doi.org/10.1371/journal.pone.0027779
dc.identifier.issn1932-6203
dc.identifier.otherPURE: 9759449
dc.identifier.otherPURE UUID: dededd15-c5aa-460f-962e-1ce713a78d12
dc.identifier.otherPubMed: 22114693
dc.identifier.otherScopus: 81155134280
dc.identifier.urihttp://hdl.handle.net/2299/16800
dc.descriptionCopyright: © 2011 Lian et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited
dc.description.abstractNCS-1 is a member of the neuronal calcium sensor (NCS) family of EF-hand Ca(2+) binding proteins which has been implicated in several physiological functions including regulation of neurotransmitter release, membrane traffic, voltage gated Ca(2+) channels, neuronal development, synaptic plasticity, and learning. NCS-1 binds to the dopamine D2 receptor, potentially affecting its internalisation and controlling dopamine D2 receptor surface expression. The D2 receptor binds NCS-1 via a short 16-residue cytoplasmic C-terminal tail. We have used NMR and fluorescence spectroscopy to characterise the interactions between the NCS-1/Ca(2+) and D2 peptide. The data show that NCS-1 binds D2 peptide with a K(d) of ∼14.3 µM and stoichiometry of peptide binding to NCS-1 of 2:1. NMR chemical shift mapping confirms that D2 peptide binds to the large, solvent-exposed hydrophobic groove, on one face of the NCS-1 molecule, with residues affected by the presence of the peptide spanning both the N and C-terminal portions of the protein. The NMR and mutagenesis data further show that movement of the C-terminal helix 11 of NCS-1 to fully expose the hydrophobic groove is important for D2 peptide binding. Molecular docking using restraints derived from the NMR chemical shift data, together with the experimentally-derived stoichiometry, produced a model of the complex between NCS-1 and the dopamine receptor, in which two molecules of the receptor are able to simultaneously bind to the NCS-1 monomer.en
dc.language.isoeng
dc.relation.ispartofPLoS ONE
dc.rightsOpen
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectCalcium Signaling
dc.subjectHumans
dc.subjectMagnetic Resonance Spectroscopy
dc.subjectModels, Molecular
dc.subjectMolecular Sequence Data
dc.subjectNeuronal Calcium-Sensor Proteins
dc.subjectNeuropeptides
dc.subjectPeptide Fragments
dc.subjectProtein Binding
dc.subjectProtein Multimerization
dc.subjectProtein Structure, Tertiary
dc.subjectRats
dc.subjectReceptors, Dopamine D2
dc.titleCharacterisation of the interaction of the C-terminus of the dopamine D2 receptor with neuronal calcium sensor-1en
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionDepartment of Human and Environmental Sciences
dc.contributor.institutionBiochemistry and Bioinformatics
dc.contributor.institutionDepartment of Biological and Environmental Sciences
dc.contributor.institutionBiosciences Research Group
dc.description.statusPeer reviewed
dc.relation.schoolSchool of Life and Medical Sciences
dc.description.versiontypeFinal Published version
dcterms.dateAccepted2011-11-16
rioxxterms.versionVoR
rioxxterms.versionofrecordhttps://doi.org/10.1371/journal.pone.0027779
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue
herts.rights.accesstypeOpen


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