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http://purl.uniprot.org/citations/34166612http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34166612http://www.w3.org/2000/01/rdf-schema#comment"Cadherin extracellular domain 1 (EC1) mediates homophilic dimerization in adherens junctions. Conserved Trp2 and Trp4 residues in type II cadherins anchor the EC1 A strand intermolecularly in strand-swapped dimers. Herein, NMR spectroscopy is used to elucidate the roles of Trp2 and Trp4 in Cadherin-11 dimerization. The monomeric state, with the A strand and Trp side chains packed intramolecularly, is in equilibrium with sparsely populated partially and fully A-strand-exposed states, in which Trp2 (and Trp4, respectively) side-chain packing is disrupted. Exchange kinetics between the major state and the partially (fully) A-strand-exposed state is slow-intermediate (intermediate-fast). A separate very fast process exchanges ordered and random-coil BC-loop conformations with populations dependent on A-strand exposure and dimerization status. In addition, very slow processes connect the folded A-strand-exposed conformation to partially unfolded states, which may represent additional domain-swapping intermediates. The dimerization mechanism of type II cadherins is revealed as coupled folding and strand swapping."xsd:string
http://purl.uniprot.org/citations/34166612http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2021.06.006"xsd:string
http://purl.uniprot.org/citations/34166612http://purl.uniprot.org/core/author"Honig B."xsd:string
http://purl.uniprot.org/citations/34166612http://purl.uniprot.org/core/author"Shapiro L."xsd:string
http://purl.uniprot.org/citations/34166612http://purl.uniprot.org/core/author"Palmer A.G."xsd:string
http://purl.uniprot.org/citations/34166612http://purl.uniprot.org/core/author"Koss H."xsd:string
http://purl.uniprot.org/citations/34166612http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34166612http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/34166612http://purl.uniprot.org/core/pages"1105-1115.e6"xsd:string
http://purl.uniprot.org/citations/34166612http://purl.uniprot.org/core/title"Dimerization of Cadherin-11 involves multi-site coupled unfolding and strand swapping."xsd:string
http://purl.uniprot.org/citations/34166612http://purl.uniprot.org/core/volume"29"xsd:string
http://purl.uniprot.org/citations/34166612http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34166612
http://purl.uniprot.org/citations/34166612http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34166612
http://purl.uniprot.org/uniprot/#_P55288-mappedCitation-34166612http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34166612
http://purl.uniprot.org/uniprot/#_Q8C7Q6-mappedCitation-34166612http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34166612
http://purl.uniprot.org/uniprot/Q8C7Q6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34166612
http://purl.uniprot.org/uniprot/P55288http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34166612