DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu A model for the solution structure of the rod arrestin tetramer. A model for the solution structure of the rod arrestin tetramer. Structure (London, England : 1993) 2008 imex curation Hanson SM., Dawson ES., Francis DJ., Van Eps N., Klug CS., Hubbell WL., Meiler J., Gurevich VV. Only protein-protein interactions in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Hanson SM., Dawson ES., Francis DJ., Van Eps N., Klug CS., Hubbell WL., Meiler J., Gurevich VV. DIP original experiment: DIP-110774X Structure (London, England : 1993) 2008 IMEx A model for the solution structure of the rod arrestin tetramer. A model for the solution structure of the rod arrestin tetramer. A model for the solution structure of the rod arrestin tetramer. Structure (London, England : 1993) 2008 imex curation Hanson SM., Dawson ES., Francis DJ., Van Eps N., Klug CS., Hubbell WL., Meiler J., Gurevich VV. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink weight by comassie molecular weight estimation by coomasie staining weight by comassie Hanson SM., Dawson ES., Francis DJ., Van Eps N., Klug CS., Hubbell WL., Meiler J., Gurevich VV. DIP original experiment: DIP-110772X Structure (London, England : 1993) 2008 IMEx A model for the solution structure of the rod arrestin tetramer. A model for the solution structure of the rod arrestin tetramer. A model for the solution structure of the rod arrestin tetramer. Structure (London, England : 1993) 2008 imex curation Hanson SM., Dawson ES., Francis DJ., Van Eps N., Klug CS., Hubbell WL., Meiler J., Gurevich VV. Only protein-protein interactions in vitro In vitro epr electron paramagnetic resonance ESR EPR EPR ESR epr predetermined predetermined participant predetermined Hanson SM., Dawson ES., Francis DJ., Van Eps N., Klug CS., Hubbell WL., Meiler J., Gurevich VV. DIP original experiment: DIP-110773X Structure (London, England : 1993) 2008 IMEx A model for the solution structure of the rod arrestin tetramer. p08168-1 S-arrestin SAG 48 kDa protein Retinal S-antigen Rod photoreceptor arrestin protein protein bovin Bos taurus (Bovine) Bovine MKANKPAPNHVIFKKISRDKSVTIYLGKRDYIDHVERVEPVDGVVLVDPELVKGKRVYVSLTCAFRYGQEDIDVMGLSFRRDLYFSQVQVFPPVGASGATTRLQESLIKKLGANTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVDFEIKAFATHSTDVEEDKIPKKSSVRLLIRKVQHAPRDMGPQPRAEASWQFFMSDKPLRLAVSLSKEIYYHGEPIPVTVAVTNSTEKTVKKIKVLVEQVTNVVLYSSDYYIKTVAAEEAQEKVPPNSSLTKTLTLVPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGIDKTVMGILVSYQIKVKLTVSGLLGELTSSEVATEVPFRLMHPQPEDPDTAKESFQDENFVFEEFARQNLKDAGEYKEEKTDQEAAMDE DIP protein P08168-1 original sequence version: 130 DIP protein P08168 original sequence version: 125 DIP protein P08168-1 original sequence version: 81 DIP protein P08168-1 original sequence version: 114 sag-1 2 4 unspecified role unspecified role unspecified role unspecified role T157C T157C half cystine half cystine Half of a disulfide bridge Dehydro certain certain sequence position certain certain certain sequence position certain D162C D162C half cystine half cystine Half of a disulfide bridge Dehydro certain certain sequence position certain certain certain sequence position certain F197C F197C half cystine half cystine Half of a disulfide bridge Dehydro certain certain sequence position certain certain certain sequence position certain A348C A348C half cystine half cystine Half of a disulfide bridge Dehydro certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction sag-2 1 4 unspecified role unspecified role unspecified role unspecified role P08168-1:p.[Phe85Ala;Phe197Ala] F85A/R1 and F197A/R1 mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F A certain certain sequence position certain certain certain sequence position certain F A Wed May 02 15:31:14 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe85ala,phe197ala' Tue Jun 30 19:30:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe85Ala;Phe197Ala]' K267R1 K267R1 r1 spin label r1 spin label mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Spin-labeling at this position decreased the strength of the interaction. F197R1 F197R1 r1 spin label r1 spin label mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Spin-labeling at this position decreased the strength of the interaction. F85R1 F85R1 r1 spin label r1 spin label mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Spin-labeling at this position decreased the strength of the interaction. F85R1 and F197R1 F85A/R1 and F197A/R1 r1 spin label r1 spin label mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F A certain certain sequence position certain certain certain sequence position certain F A Spin-labeling at this position fully disrupted the interaction. ecolx Escherichia coli direct interaction direct interaction sag-sag-1 3 4 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 4 unspecified role unspecified role unspecified role unspecified role M75R1 M75R1 r1 spin label r1 spin label certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction