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http://purl.uniprot.org/citations/32327662http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32327662http://www.w3.org/2000/01/rdf-schema#comment"Plexins are receptors for semaphorins that transduce signals for regulating neuronal development and other processes. Plexins are single-pass transmembrane proteins with multiple domains in both the extracellular and intracellular regions. Semaphorin activates plexin by binding to its extracellular N-terminal Sema domain, inducing the active dimer of the plexin intracellular region. The mechanism underlying this activation process of plexin is incompletely understood. We present cryo-electron microscopic structure of full-length human PlexinC1 in complex with the viral semaphorin mimic A39R. The structure shows that A39R induces a specific dimer of PlexinC1 where the membrane-proximal domains from the two PlexinC1 protomers are placed close to each other, poised to promote the active dimer of the intracellular region. This configuration is imposed by a distinct conformation of the PlexinC1 extracellular region, stabilized by inter-domain interactions among the Sema and membrane-proximal domains. Our mutational analyses support the critical role of this conformation in PlexinC1 activation."xsd:string
http://purl.uniprot.org/citations/32327662http://purl.org/dc/terms/identifier"doi:10.1038/s41467-020-15862-0"xsd:string
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/author"Chen H."xsd:string
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/author"Zhang X."xsd:string
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/author"Tian H."xsd:string
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/author"Shang G."xsd:string
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/author"Bai X.C."xsd:string
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/author"Kuo Y.C."xsd:string
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/author"Uchikawa E."xsd:string
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/name"Nat Commun"xsd:string
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/pages"1953"xsd:string
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/title"Cryo-EM structure of the PlexinC1/A39R complex reveals inter-domain interactions critical for ligand-induced activation."xsd:string
http://purl.uniprot.org/citations/32327662http://purl.uniprot.org/core/volume"11"xsd:string
http://purl.uniprot.org/citations/32327662http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/32327662
http://purl.uniprot.org/citations/32327662http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/32327662
http://purl.uniprot.org/uniprot/#_O60486-mappedCitation-32327662http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32327662
http://purl.uniprot.org/uniprot/#_Q8JL80-mappedCitation-32327662http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/32327662
http://purl.uniprot.org/uniprot/Q8JL80http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32327662
http://purl.uniprot.org/uniprot/O60486http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/32327662