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http://purl.uniprot.org/citations/16615918http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16615918http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16615918http://www.w3.org/2000/01/rdf-schema#comment"The Na+/H+ exchanger regulatory factor (NHERF) is a key adaptor protein involved in the anchoring of ion channels and receptors to the actin cytoskeleton through binding to ERM (ezrin/radixin/moesin) proteins. NHERF binds the FERM domain of ERM proteins, although NHERF has no signature Motif-1 sequence for FERM binding found in adhesion molecules. The crystal structures of the radixin FERM domain complexed with the NHERF-1 and NHERF-2 C-terminal peptides revealed a peptide binding site of the FERM domain specific for the 13 residue motif MDWxxxxx(L/I)Fxx(L/F) (Motif-2), which is distinct from Motif-1. This Motif-2 forms an amphipathic alpha helix for hydrophobic docking to subdomain C of the FERM domain. This docking causes induced-fit conformational changes in subdomain C and affects binding to adhesion molecule peptides, while the two binding sites are not overlapped. Our studies provide structural paradigms for versatile ERM linkages between membrane proteins and the cytoskeleton."xsd:string
http://purl.uniprot.org/citations/16615918http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2006.01.015"xsd:string
http://purl.uniprot.org/citations/16615918http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2006.01.015"xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/author"Hakoshima T."xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/author"Hakoshima T."xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/author"Terawaki S."xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/author"Terawaki S."xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/author"Maesaki R."xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/author"Maesaki R."xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/pages"777-789"xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/pages"777-789"xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/title"Structural basis for NHERF recognition by ERM proteins."xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/title"Structural basis for NHERF recognition by ERM proteins."xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/16615918http://purl.uniprot.org/core/volume"14"xsd:string
http://purl.uniprot.org/citations/16615918http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16615918
http://purl.uniprot.org/citations/16615918http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16615918
http://purl.uniprot.org/citations/16615918http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16615918
http://purl.uniprot.org/citations/16615918http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16615918