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http://purl.uniprot.org/citations/30853411http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30853411http://www.w3.org/2000/01/rdf-schema#comment"The Dedicator Of CytoKinesis (DOCK) family of atypical guanine nucleotide exchange factors activates the Rho family GTPases Rac and/or Cdc42 through DOCK homology region 2 (DHR-2). Previous structural analyses of the DHR-2 domains of DOCK2 and DOCK9 have shown that they preferentially bind Rac1 and Cdc42, respectively; however, the molecular mechanism by which DHR-2 distinguishes between these GTPases is unclear. Here we report the crystal structure of the Cdc42-bound form of the DOCK7 DHR-2 domain showing dual specificity for Rac1 and Cdc42. The structure revealed increased substrate tolerance of DOCK7 at the interfaces with switch 1 and residue 56 of Cdc42. Furthermore, molecular dynamics simulations showed a closed-to-open conformational change in the DOCK7 DHR-2 domain between the Cdc42- and Rac1-bound states by lobe B displacement. Our results suggest that lobe B acts as a sensor for identifying different switch 1 conformations and explain how DOCK7 recognizes both Rac1 and Cdc42."xsd:string
http://purl.uniprot.org/citations/30853411http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2019.02.001"xsd:string
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/author"Ihara K."xsd:string
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/author"Shirouzu M."xsd:string
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/author"Tsuda K."xsd:string
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/author"Honda K."xsd:string
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/author"Ohsawa N."xsd:string
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/author"Kukimoto-Niino M."xsd:string
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/author"Mishima-Tsumagari C."xsd:string
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/pages"741-748.e3"xsd:string
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/title"Structural Basis for the Dual Substrate Specificity of DOCK7 Guanine Nucleotide Exchange Factor."xsd:string
http://purl.uniprot.org/citations/30853411http://purl.uniprot.org/core/volume"27"xsd:string
http://purl.uniprot.org/citations/30853411http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/30853411
http://purl.uniprot.org/citations/30853411http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/30853411
http://purl.uniprot.org/uniprot/#_P52735-mappedCitation-30853411http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30853411
http://purl.uniprot.org/uniprot/#_Q07889-mappedCitation-30853411http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30853411
http://purl.uniprot.org/uniprot/#_Q07890-mappedCitation-30853411http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30853411
http://purl.uniprot.org/uniprot/#_Q14155-mappedCitation-30853411http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30853411
http://purl.uniprot.org/uniprot/#_Q14185-mappedCitation-30853411http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30853411
http://purl.uniprot.org/uniprot/#_Q15052-mappedCitation-30853411http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30853411
http://purl.uniprot.org/uniprot/#_A1L390-mappedCitation-30853411http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30853411
http://purl.uniprot.org/uniprot/#_A4FU72-mappedCitation-30853411http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/30853411