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http://purl.uniprot.org/citations/15296743http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15296743http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15296743http://www.w3.org/2000/01/rdf-schema#comment"The C-terminal G3 domains of lecticans mediate crosslinking to diverse extracellular matrix (ECM) proteins during ECM assembly, through their C-type lectin (CLD) subdomains. The structure of the rat aggrecan CLD in a Ca(2+)-dependent complex with fibronectin type III repeats 3-5 of rat tenascin-R provides detailed support for such crosslinking. The CLD loops bind Ca2+ like other CLDs, but no carbohydrate binding is observed or possible. This is thus the first example of a direct Ca(2+)-dependent protein-protein interaction of a CLD. Surprisingly, tenascin-R does not coordinate the Ca2+ ions directly. Electron microscopy confirms that full-length tenascin-R and tenascin-C crosslink hyaluronan-aggrecan complexes. The results are significant for the binding of all lectican CLDs to tenascin-R and tenascin-C. Comparison of the protein interaction surface with that of P-selectin in complex with the PGSL-1 peptide suggests that direct protein-protein interactions of Ca(2+)-binding CLDs may be more widespread than previously appreciated."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2004.05.021"xsd:string
http://purl.uniprot.org/citations/15296743http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2004.05.021"xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"Logan D.T."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"Logan D.T."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"Morgelin M."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"Morgelin M."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"Aspberg A."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"Aspberg A."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"Olin A.I."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"Olin A.I."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"Lundell A."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"Lundell A."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"al-Karadaghi S."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/author"al-Karadaghi S."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/pages"1495-1506"xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/pages"1495-1506"xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/title"Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins."xsd:string
http://purl.uniprot.org/citations/15296743http://purl.uniprot.org/core/title"Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins."xsd:string