| http://purl.uniprot.org/citations/15663004 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15663004 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15663004 | http://www.w3.org/2000/01/rdf-schema#comment | "PDZ domains are protein-protein interaction modules that are crucial for the assembly of structural and signaling complexes. PDZ domains specifically bind short carboxyl-terminal peptides and occasionally internal sequences that structurally resemble peptide termini. Previously, using yeast two-hybrid methodology, we studied the interaction of two PDZ domains present in the large submembranous protein tyrosine phosphatase PTP-BL with' the C-terminal half of the LIM domain-containing protein RIL. Deletion of the extreme RIL C-terminus did not eliminate binding, suggesting the presence of a PDZ binding site within the RIL LIM moiety. We have now performed experiments in mammalian cell lysates and found that the RIL C-terminus proper, but not the RIL LIM domain, can interact with PTP-BL, albeit very weakly. However, this interaction with PTP-BL PDZ domains is greatly enhanced when the combined RIL LIM domain and C-terminus is used, pointing to synergistic effects. NMR titration experiments and site-directed mutagenesis indicate that this result is not dependent on specific interactions that require surface exposed residues on the RIL LIM domain, suggesting a stabilizing role in the association with PTP-BL."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.org/dc/terms/identifier | "doi:10.1007/s11033-005-1407-8"xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.org/dc/terms/identifier | "doi:10.1007/s11033-005-1407-8"xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "Vuister G.W."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "Vuister G.W."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "Aelen J."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "Aelen J."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "Hendriks W.J."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "Hendriks W.J."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "Walma T."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "Walma T."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "te Lindert M.M."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "te Lindert M.M."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "van Ham M.A."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "van Ham M.A."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "van den Berk L.C."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/author | "van den Berk L.C."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/name | "Mol. Biol. Rep."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/name | "Mol. Biol. Rep."xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/pages | "203-215"xsd:string |
| http://purl.uniprot.org/citations/15663004 | http://purl.uniprot.org/core/pages | "203-215"xsd:string |