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http://purl.uniprot.org/citations/18940602http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18940602http://www.w3.org/2000/01/rdf-schema#comment"Calcium influx drives two opposing voltage-activated calcium channel (Ca(V)) self-modulatory processes: calcium-dependent inactivation (CDI) and calcium-dependent facilitation (CDF). Specific Ca(2+)/calmodulin (Ca(2+)/CaM) lobes produce CDI and CDF through interactions with the Ca(V)alpha(1) subunit IQ domain. Curiously, Ca(2+)/CaM lobe modulation polarity appears inverted between Ca(V)1s and Ca(V)2s. Here, we present crystal structures of Ca(V)2.1, Ca(V)2.2, and Ca(V)2.3 Ca(2+)/CaM-IQ domain complexes. All display binding orientations opposite to Ca(V)1.2 with a physical reversal of the CaM lobe positions relative to the IQ alpha-helix. Titration calorimetry reveals lobe competition for a high-affinity site common to Ca(V)1 and Ca(V)2 IQ domains that is occupied by the CDI lobe in the structures. Electrophysiological experiments demonstrate that the N-terminal Ca(V)2 Ca(2+)/C-lobe anchors affect CDF. Together, the data unveil the remarkable structural plasticity at the heart of Ca(V) feedback modulation and indicate that Ca(V)1 and Ca(V)2 IQ domains bear a dedicated CDF site that exchanges Ca(2+)/CaM lobe occupants."xsd:string
http://purl.uniprot.org/citations/18940602http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2008.07.010"xsd:string
http://purl.uniprot.org/citations/18940602http://purl.uniprot.org/core/author"Fujiwara Y."xsd:string
http://purl.uniprot.org/citations/18940602http://purl.uniprot.org/core/author"Kim E.Y."xsd:string
http://purl.uniprot.org/citations/18940602http://purl.uniprot.org/core/author"Van Petegem F."xsd:string
http://purl.uniprot.org/citations/18940602http://purl.uniprot.org/core/author"Minor D.L. Jr."xsd:string
http://purl.uniprot.org/citations/18940602http://purl.uniprot.org/core/author"Cooley E.S."xsd:string
http://purl.uniprot.org/citations/18940602http://purl.uniprot.org/core/author"Rumpf C.H."xsd:string
http://purl.uniprot.org/citations/18940602http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18940602http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/18940602http://purl.uniprot.org/core/pages"1455-1467"xsd:string
http://purl.uniprot.org/citations/18940602http://purl.uniprot.org/core/title"Structures of CaV2 Ca2+/CaM-IQ domain complexes reveal binding modes that underlie calcium-dependent inactivation and facilitation."xsd:string
http://purl.uniprot.org/citations/18940602http://purl.uniprot.org/core/volume"16"xsd:string
http://purl.uniprot.org/citations/18940602http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18940602
http://purl.uniprot.org/citations/18940602http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18940602
http://purl.uniprot.org/uniprot/#_P0DP23-mappedCitation-18940602http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18940602
http://purl.uniprot.org/uniprot/#_Q07652-mappedCitation-18940602http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18940602
http://purl.uniprot.org/uniprot/#_P27884-mappedCitation-18940602http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18940602
http://purl.uniprot.org/uniprot/#_Q05152-mappedCitation-18940602http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18940602
http://purl.uniprot.org/uniprot/P27884http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18940602
http://purl.uniprot.org/uniprot/Q07652http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18940602
http://purl.uniprot.org/uniprot/P0DP23http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18940602
http://purl.uniprot.org/uniprot/Q05152http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18940602