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http://purl.uniprot.org/citations/17151196http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17151196http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17151196http://www.w3.org/2000/01/rdf-schema#comment"A 2.5-A resolution structure of calcium-free calmodulin (CaM) bound to the first two IQ motifs of the murine myosin V heavy chain reveals an unusual CaM conformation. The C-terminal lobe of each CaM adopts a semi-open conformation that grips the first part of the IQ motif (IQxxxR), whereas the N-terminal lobe adopts a closed conformation that interacts more weakly with the second part of the motif (GxxxR). Variable residues in the IQ motif play a critical role in determining the precise structure of the bound CaM, such that even the consensus residues of different motifs show unique interactions with CaM. This complex serves as a model for the lever arm region of many classes of unconventional myosins, as well as other IQ motif-containing proteins such as neuromodulin and IQGAPs."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0609436103"xsd:string
http://purl.uniprot.org/citations/17151196http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0609436103"xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Gaucher J.F."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Gaucher J.F."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Houdusse A."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Houdusse A."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Trybus K.M."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Trybus K.M."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Mui S."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Mui S."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Cohen C."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Cohen C."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Krementsova E."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/author"Krementsova E."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/pages"19326-19331"xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/pages"19326-19331"xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/title"Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features."xsd:string
http://purl.uniprot.org/citations/17151196http://purl.uniprot.org/core/title"Crystal structure of apo-calmodulin bound to the first two IQ motifs of myosin V reveals essential recognition features."xsd:string