http://purl.uniprot.org/citations/26165597 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/26165597 | http://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/26165597 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.str.2015.06.003"xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Acton T.B."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Janjua H."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Montelione G.T."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Su M."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Seetharaman J."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Tong L."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Xiao R."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Huang Y.J."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Aramini J.M."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Vorobiev S.M."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Campbell E.T."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/author | "Tuberty L.M."xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/date | "2015"xsd:gYear |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
http://purl.uniprot.org/citations/26165597 | http://purl.uniprot.org/core/pages | "1382-1393"xsd:string |
http://purl.uniprot.org/citations/26165597 | http://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/26165597 | http://purl.uniprot.org/core/volume | "23"xsd:string |
http://purl.uniprot.org/citations/26165597 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/26165597 |
http://purl.uniprot.org/citations/26165597 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/26165597 |
http://purl.uniprot.org/uniprot/#_Q16525-mappedCitation-26165597 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26165597 |
http://purl.uniprot.org/uniprot/#_Q14007-mappedCitation-26165597 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26165597 |
http://purl.uniprot.org/uniprot/#_Q71SP6-mappedCitation-26165597 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/26165597 |