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http://purl.uniprot.org/citations/23519214http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23519214http://www.w3.org/2000/01/rdf-schema#comment"Kinesin-mediated cargo transport is required for many cellular functions and plays a key role in pathological processes. Structural information on how kinesins recognize their cargoes is required for a molecular understanding of this fundamental and ubiquitous process. Here, we present the crystal structure of the tetratricopeptide repeat domain of kinesin light chain 2 in complex with a cargo peptide harboring a "tryptophan-acidic" motif derived from SKIP (SifA-kinesin interacting protein), a critical host determinant in Salmonella pathogenesis and a regulator of lysosomal positioning. Structural data together with biophysical, biochemical, and cellular assays allow us to propose a framework for intracellular transport based on the binding by kinesin-1 of W-acidic cargo motifs through a combination of electrostatic interactions and sequence-specific elements, providing direct molecular evidence of the mechanisms for kinesin-1:cargo recognition."xsd:string
http://purl.uniprot.org/citations/23519214http://purl.org/dc/terms/identifier"doi:10.1126/science.1234264"xsd:string
http://purl.uniprot.org/citations/23519214http://purl.uniprot.org/core/author"Lamprecht A."xsd:string
http://purl.uniprot.org/citations/23519214http://purl.uniprot.org/core/author"Dodding M.P."xsd:string
http://purl.uniprot.org/citations/23519214http://purl.uniprot.org/core/author"Steiner R.A."xsd:string
http://purl.uniprot.org/citations/23519214http://purl.uniprot.org/core/author"Pernigo S."xsd:string
http://purl.uniprot.org/citations/23519214http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23519214http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/23519214http://purl.uniprot.org/core/pages"356-359"xsd:string
http://purl.uniprot.org/citations/23519214http://purl.uniprot.org/core/title"Structural basis for kinesin-1:cargo recognition."xsd:string
http://purl.uniprot.org/citations/23519214http://purl.uniprot.org/core/volume"340"xsd:string
http://purl.uniprot.org/citations/23519214http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23519214
http://purl.uniprot.org/citations/23519214http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23519214
http://purl.uniprot.org/uniprot/#_D3YXZ3-mappedCitation-23519214http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23519214
http://purl.uniprot.org/uniprot/#_D3Z5Y7-mappedCitation-23519214http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23519214
http://purl.uniprot.org/uniprot/#_O88447-mappedCitation-23519214http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23519214
http://purl.uniprot.org/uniprot/#_O88448-mappedCitation-23519214http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23519214
http://purl.uniprot.org/uniprot/#_Q9ER39-mappedCitation-23519214http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23519214
http://purl.uniprot.org/uniprot/#_Q8IWE5-mappedCitation-23519214http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23519214
http://purl.uniprot.org/uniprot/#_Q91YS4-mappedCitation-23519214http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23519214
http://purl.uniprot.org/uniprot/#_Q9UQF2-mappedCitation-23519214http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/23519214
http://purl.uniprot.org/uniprot/O88447http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23519214
http://purl.uniprot.org/uniprot/Q91YS4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23519214
http://purl.uniprot.org/uniprot/Q8IWE5http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/23519214