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http://purl.uniprot.org/citations/2973411http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2973411http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/2973411http://www.w3.org/2000/01/rdf-schema#comment"Protein I is a hetero-tetramer which contains two copies each of p11 and p36. p36 (calpactin I, lipocortin II) is a major substrate of retrovirally encoded tyrosine protein kinases, while p11 modulates several Ca2+-induced properties also displayed by p36 alone. Here we have characterized the p11 binding site on p36 by fluorescence spectroscopy using porcine p36 labelled at cysteine 8 with the fluorophore Prodan (6-proprionyl-2-dimethylamino-naphthalene). We have used peptides of differing length from the amino-terminal domain of p36 to restrict the major binding site to the first 12 residues. Noticeable binding is still observed with a peptide containing only the first nine residues. Interestingly the N-terminal acetyl group of p36 forms a functional part of the p11 binding site. CD studies indicate that the binding region can form an alpha-helix, which seems to have amphiphatic properties when projected on a helical wheel. This structural element is also known for a calmodulin binding protein. Thus the question is raised whether other p11/calmodulin-related proteins interact with their target proteins via a similar mechanism. We also discuss how p11 could modulate p36 associated properties."xsd:string
http://purl.uniprot.org/citations/2973411http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1988.tb03089.x"xsd:string
http://purl.uniprot.org/citations/2973411http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1988.tb03089.x"xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/author"Weber K."xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/author"Weber K."xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/author"Marriott G."xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/author"Marriott G."xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/author"Johnsson N."xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/author"Johnsson N."xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/date"1988"xsd:gYear
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/pages"2435-2442"xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/pages"2435-2442"xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/title"p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphipathic helix."xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/title"p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphipathic helix."xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/2973411http://purl.uniprot.org/core/volume"7"xsd:string
http://purl.uniprot.org/citations/2973411http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2973411
http://purl.uniprot.org/citations/2973411http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/2973411
http://purl.uniprot.org/citations/2973411http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2973411
http://purl.uniprot.org/citations/2973411http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/2973411