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Article: Interaction between calcium-free calmodulin and IQ motif of neurogranin studied by nuclear magnetic resonance spectroscopy

TitleInteraction between calcium-free calmodulin and IQ motif of neurogranin studied by nuclear magnetic resonance spectroscopy
Authors
Issue Date2003
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yabio
Citation
Analytical Biochemistry, 2003, v. 315 n. 2, p. 175-182 How to Cite?
AbstractThe interaction of Ca 2+-free calmodulin (apoCaM) with the IQ motif corresponding to the calmodulin-binding domain of neurogranin has been studied by nuclear magnetic resonance (NMR) methods. The NMR spectra of uncomplexed apoCaM and apoCaM in complex with the IQ motif recorded at 750MHz were studied and the backbone assignments of the protein in both forms were obtained by triple-resonance multidimensional NMR experiments. Chemical shift perturbations were used to map the binding surfaces. Only a single set of resonances was observed throughout the titration, indicating that the binding interaction is under fast exchange. Analysis of chemical shift changes indicates that (a) the main interaction and conformational changes occur in the C-terminal domain of calmodulin and (b) linker-1 (residues 40-44) between EF-1 and EF-2, linker-3 (residues 112-117) between EF-3 and EF-4, and the end of the α-helix H (residues 145-148) may be involved in the binding process. The dissociation constant (K d), estimated by fitting the chemical shift changes against the IQ peptide concentration, ranged from about 1.2×10 -5 to 8.8×10 -5M. This result demonstrates that the interaction falls into the weak binding regime. © 2003 Elsevier Science (USA). All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/157355
ISSN
2015 Impact Factor: 2.243
2015 SCImago Journal Rankings: 0.725
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorCui, Yen_US
dc.contributor.authorWen, Jen_US
dc.contributor.authorSze, KHen_US
dc.contributor.authorMan, Den_US
dc.contributor.authorLin, Den_US
dc.contributor.authorLiu, Men_US
dc.contributor.authorZhu, Gen_US
dc.date.accessioned2012-08-08T08:49:11Z-
dc.date.available2012-08-08T08:49:11Z-
dc.date.issued2003en_US
dc.identifier.citationAnalytical Biochemistry, 2003, v. 315 n. 2, p. 175-182en_US
dc.identifier.issn0003-2697en_US
dc.identifier.urihttp://hdl.handle.net/10722/157355-
dc.description.abstractThe interaction of Ca 2+-free calmodulin (apoCaM) with the IQ motif corresponding to the calmodulin-binding domain of neurogranin has been studied by nuclear magnetic resonance (NMR) methods. The NMR spectra of uncomplexed apoCaM and apoCaM in complex with the IQ motif recorded at 750MHz were studied and the backbone assignments of the protein in both forms were obtained by triple-resonance multidimensional NMR experiments. Chemical shift perturbations were used to map the binding surfaces. Only a single set of resonances was observed throughout the titration, indicating that the binding interaction is under fast exchange. Analysis of chemical shift changes indicates that (a) the main interaction and conformational changes occur in the C-terminal domain of calmodulin and (b) linker-1 (residues 40-44) between EF-1 and EF-2, linker-3 (residues 112-117) between EF-3 and EF-4, and the end of the α-helix H (residues 145-148) may be involved in the binding process. The dissociation constant (K d), estimated by fitting the chemical shift changes against the IQ peptide concentration, ranged from about 1.2×10 -5 to 8.8×10 -5M. This result demonstrates that the interaction falls into the weak binding regime. © 2003 Elsevier Science (USA). All rights reserved.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yabioen_US
dc.relation.ispartofAnalytical Biochemistryen_US
dc.subject.meshAmino Acid Motifsen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshApoproteins - Metabolismen_US
dc.subject.meshBinding Sitesen_US
dc.subject.meshCalcium - Metabolismen_US
dc.subject.meshCalmodulin - Metabolismen_US
dc.subject.meshCalmodulin-Binding Proteins - Chemistry - Metabolismen_US
dc.subject.meshCattleen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshNerve Tissue Proteins - Chemistry - Metabolismen_US
dc.subject.meshNeurograninen_US
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.subject.meshThermodynamicsen_US
dc.titleInteraction between calcium-free calmodulin and IQ motif of neurogranin studied by nuclear magnetic resonance spectroscopyen_US
dc.typeArticleen_US
dc.identifier.emailSze, KH:khsze@hku.hken_US
dc.identifier.authoritySze, KH=rp00785en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0003-2697(03)00007-1en_US
dc.identifier.pmid12689827-
dc.identifier.scopuseid_2-s2.0-0037446203en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037446203&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume315en_US
dc.identifier.issue2en_US
dc.identifier.spage175en_US
dc.identifier.epage182en_US
dc.identifier.isiWOS:000182332000005-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridCui, Y=7402595826en_US
dc.identifier.scopusauthoridWen, J=55240716400en_US
dc.identifier.scopusauthoridSze, KH=7006735061en_US
dc.identifier.scopusauthoridMan, D=36878997300en_US
dc.identifier.scopusauthoridLin, D=9036520900en_US
dc.identifier.scopusauthoridLiu, M=7406299908en_US
dc.identifier.scopusauthoridZhu, G=7402633110en_US

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