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http://purl.uniprot.org/citations/26165597http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26165597http://www.w3.org/2000/01/rdf-schema#comment"RAS binding is a critical step in the activation of BRAF protein serine/threonine kinase and stimulation of the mitogen-activated protein kinase signaling pathway. Mutations in both RAS and BRAF are associated with many human cancers. Here, we report the solution nuclear magnetic resonance (NMR) and X-ray crystal structures of the RAS-binding domain (RBD) from human BRAF. We further studied the complex between BRAF RBD and the GppNHp bound form of HRAS in solution. Backbone, side-chain, and (19)F NMR chemical shift perturbations reveal unexpected changes distal to the RAS-binding face that extend through the core of the RBD structure. Moreover, backbone amide hydrogen/deuterium exchange NMR data demonstrate conformational ensemble changes in the RBD core structure upon complex formation. These changes in BRAF RBD reveal a basis for allosteric regulation of BRAF structure and function, and suggest a mechanism by which RAS binding can signal the drastic domain rearrangements required for activation of BRAF kinase."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2015.06.003"xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Acton T.B."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Janjua H."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Montelione G.T."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Su M."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Seetharaman J."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Tong L."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Xiao R."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Huang Y.J."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Aramini J.M."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Vorobiev S.M."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Campbell E.T."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/author"Tuberty L.M."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/pages"1382-1393"xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/title"The RAS-Binding Domain of Human BRAF Protein Serine/Threonine Kinase Exhibits Allosteric Conformational Changes upon Binding HRAS."xsd:string
http://purl.uniprot.org/citations/26165597http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/26165597http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/26165597
http://purl.uniprot.org/citations/26165597http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/26165597
http://purl.uniprot.org/uniprot/#_Q16525-mappedCitation-26165597http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26165597
http://purl.uniprot.org/uniprot/#_Q14007-mappedCitation-26165597http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26165597
http://purl.uniprot.org/uniprot/#_Q71SP6-mappedCitation-26165597http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/26165597