http://purl.uniprot.org/citations/16147993 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16147993 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/16147993 | http://www.w3.org/2000/01/rdf-schema#comment | "LIN-2/7 (L27) domains are protein interaction modules that preferentially hetero-oligomerize, a property critical for their function in directing specific assembly of supramolecular signaling complexes at synapses and other polarized cell-cell junctions. We have solved the solution structure of the heterodimer composed of the L27 domains from LIN-2 and LIN-7. Comparison of this structure with other L27 domain structures has allowed us to formulate a general model for why most L27 domains form an obligate heterodimer complex. L27 domains can be divided in two types (A and B), with each heterodimer comprising an A/B pair. We have identified two keystone positions that play a central role in discrimination. The residues at these positions are energetically acceptable in the context of an A/B heterodimer, but would lead to packing defects or electrostatic repulsion in the context of A/A and B/B homodimers. As predicted by the model, mutations of keystone residues stabilize normally strongly disfavored homodimers. Thus, L27 domains are specifically optimized to avoid homodimeric interactions."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.M506536200"xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m506536200"xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/author | "Lim W.A."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/author | "Lim W.A."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/author | "Ou H.D."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/author | "Ou H.D."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/author | "Dotsch V."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/author | "Dotsch V."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/author | "Lohr F."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/author | "Lohr F."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/author | "Petrosky K.Y."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/author | "Petrosky K.Y."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/pages | "38528-38536"xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/pages | "38528-38536"xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/title | "A general model for preferential hetero-oligomerization of LIN-2/7 domains: mechanism underlying directed assembly of supramolecular signaling complexes."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/title | "A general model for preferential hetero-oligomerization of LIN-2/7 domains: mechanism underlying directed assembly of supramolecular signaling complexes."xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/volume | "280"xsd:string |
http://purl.uniprot.org/citations/16147993 | http://purl.uniprot.org/core/volume | "280"xsd:string |