RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/23798443http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23798443http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23798443http://www.w3.org/2000/01/rdf-schema#comment"Class V myosins (MyoV), the most studied unconventional myosins, recognize numerous cargos mainly via the motor's globular tail domain (GTD). Little is known regarding how MyoV-GTD recognizes such a diverse array of cargos specifically. Here, we solved the crystal structures of MyoVa-GTD in its apo-form and in complex with two distinct cargos, melanophilin and Rab interacting lysosomal protein-like 2. The apo-MyoVa-GTD structure indicates that most mutations found in patients with Griscelli syndrome, microvillus inclusion disease, or cancers or in "dilute" rodents likely impair the folding of GTD. The MyoVa-GTD/cargo complex structure reveals two distinct cargo-binding surfaces, one primarily via charge-charge interaction and the other mainly via hydrophobic interactions. Structural and biochemical analysis reveal the specific cargo-binding specificities of various isoforms of mammalian MyoV as well as very different cargo recognition mechanisms of MyoV between yeast and higher eukaryotes. The MyoVa-GTD structures resolved here provide a framework for future functional studies of vertebrate class V myosins."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1306768110"xsd:string
http://purl.uniprot.org/citations/23798443http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1306768110"xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/author"Liu X."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/author"Liu X."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/author"Wei Z."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/author"Wei Z."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/author"Yu C."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/author"Yu C."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/author"Zhang M."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/author"Zhang M."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/pages"11314-11319"xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/pages"11314-11319"xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/title"Structural basis of cargo recognitions for class V myosins."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/title"Structural basis of cargo recognitions for class V myosins."xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/volume"110"xsd:string
http://purl.uniprot.org/citations/23798443http://purl.uniprot.org/core/volume"110"xsd:string
http://purl.uniprot.org/citations/23798443http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23798443
http://purl.uniprot.org/citations/23798443http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23798443