DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Atomic structure of the autosomal recessive hypercholesterolemia phosphotyrosine-binding domain in complex with the LDL-receptor tail. Atomic structure of the autosomal recessive hypercholesterolemia phosphotyrosine-binding domain in complex with the LDL-receptor tail. Proceedings of the National Academy of Sciences of the United States of America 2012 imex curation Dvir H., Shah M., Girardi E., Guo L., Farquhar MG., Zajonc DM. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Dvir H., Shah M., Girardi E., Guo L., Farquhar MG., Zajonc DM. DIP original experiment: DIP-251639X Proceedings of the National Academy of Sciences of the United States of America 2012 IMEx Atomic structure of the autosomal recessive hypercholesterolemia phosphotyrosine-binding domain in complex with the LDL-receptor tail. Atomic structure of the autosomal recessive hypercholesterolemia phosphotyrosine-binding domain in complex with the LDL-receptor tail. Atomic structure of the autosomal recessive hypercholesterolemia phosphotyrosine-binding domain in complex with the LDL-receptor tail. Proceedings of the National Academy of Sciences of the United States of America 2012 imex curation Dvir H., Shah M., Girardi E., Guo L., Farquhar MG., Zajonc DM. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Dvir H., Shah M., Girardi E., Guo L., Farquhar MG., Zajonc DM. DIP original experiment: DIP-251640X Proceedings of the National Academy of Sciences of the United States of America 2012 IMEx Atomic structure of the autosomal recessive hypercholesterolemia phosphotyrosine-binding domain in complex with the LDL-receptor tail. Atomic structure of the autosomal recessive hypercholesterolemia phosphotyrosine-binding domain in complex with the LDL-receptor tail. Atomic structure of the autosomal recessive hypercholesterolemia phosphotyrosine-binding domain in complex with the LDL-receptor tail. Proceedings of the National Academy of Sciences of the United States of America 2012 imex curation Dvir H., Shah M., Girardi E., Guo L., Farquhar MG., Zajonc DM. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Dvir H., Shah M., Girardi E., Guo L., Farquhar MG., Zajonc DM. DIP original experiment: DIP-251641X Proceedings of the National Academy of Sciences of the United States of America 2012 IMEx Atomic structure of the autosomal recessive hypercholesterolemia phosphotyrosine-binding domain in complex with the LDL-receptor tail. arh_rat Low density lipoprotein receptor adapter protein 1 Ldlrap1 Arh Autosomal recessive hypercholesterolemia protein homolog protein protein rat Rattus norvegicus (Rat) Rat MDALKSAGRALIRSPSLAKQSWAGGRHRKLPENWTDTRETLLEGMVFSLKYLGMTLVERPKGEELSAAAVKRIVATAKASGKKLQKVTLKVSPRGIILTDSLTSQLIENVSIYRISYCTAQMHDKVFAYIAQSQQNESLECHAFLCTKRKVAQAVTLTVAQAFKVAFEFWQVSKEEKEKREKANQEGGDVPGTRRDSTPSLKTSVATGNLLDLEELAKAPLSTVSANTKNMDDALRPQVLGNNSVVWELDDGLDEAFSRLAQSRTNPQVLDTGLTAQDIHYAQCLSPTDWDKPDSSGFDQDDVFSF DIP protein D3ZAR1 original sequence version: 29 FD73C718AED585F5 ldlr_human Low-density lipoprotein receptor LDLR protein protein human Homo sapiens Human MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDIDECQDPDTCSQLCVNLEGGYKCQCEEGFQLDPHTKACKAVGSIAYLFFTNRHEVRKMTLDRSEYTSLIPNLRNVVALDTEVASNRIYWSDLSQRMICSTQLDRAHGVSSYDTVISRDIQAPDGLAVDWIHSNIYWTDSVLGTVSVADTKGVKRKTLFRENGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTENIQWPNGITLDLLSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKRLAHPFSLAVFEDKVFWTDIINEAIFSANRLTGSDVNLLAENLLSPEDMVLFHNLTQPRGVNWCERTTLSNGGCQYLCLPAPQINPHSPKFTCACPDGMLLARDMRSCLTEAEAAVATQETSTVRLKVSSTAVRTQHTTTRPVPDTSRLPGATPGLTTVEIVTMSHQALGDVAGRGNEKKPSSVRALSIVLPIVLLVFLCLGVFLLWKNWRLKNINSINFDNPVYQKTTEDEVHICHNQDGYSYPSRQMVSLEDDVA DIP protein P01130 original sequence version: 115 DIP protein P01130 original sequence version: 122 DIP protein P01130 original sequence version: 140 DIP protein P01130 original sequence version: 173 A4C28E9B8BADAD5E ldlr-ldlrap1-1 1 5 unspecified role unspecified role unspecified role unspecified role Region 819-832 Region 819-832 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 4 unspecified role unspecified role unspecified role unspecified role Region 43-174 Region 43-174 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction ldlr-ldlrap1-2 3 5 unspecified role unspecified role bait bait Biotin-tag Biotin-tag biotin tag biotin tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range Region 820-831 Region 820-831 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 4 unspecified role unspecified role prey prey Region 29-197 Region 29-197 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain D3ZAR1:p.Thr55Met T55M mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain T M This feature has been corrected as a result of our quality control procedures. The original label was 'T55M'. Wed May 02 15:25:49 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr55met' Tue Jun 30 15:50:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr55Met' ecolx Escherichia coli direct interaction direct interaction ldlr-ldlrap1-3 2 5 unspecified role unspecified role bait bait Region 820-831 Region 820-831 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain Biotin-tag Biotin-tag biotin tag biotin tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range P01130:p.Tyr828Cys Y828C mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain Y C This feature has been corrected as a result of our quality control procedures. The original label was 'Y828C'. Wed May 02 18:00:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr828cys' Tue Jun 30 17:40:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr828Cys' P01130:p.Gln829Ala Q829A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Q A This feature has been corrected as a result of our quality control procedures. The original label was 'Q829A'. Wed May 02 14:41:32 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln829ala' Tue Jun 30 17:31:20 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln829Ala' P01130:p.Ile821Arg I821R mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain I R This feature has been corrected as a result of our quality control procedures. The original label was 'I821R'. Wed May 02 19:49:37 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile821arg' Tue Jun 30 18:25:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile821Arg' P01130:p.Ile821Ala I821A mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain I A This feature has been corrected as a result of our quality control procedures. The original label was 'I821A'. Wed May 02 19:47:13 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile821ala' Tue Jun 30 17:09:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile821Ala' in vitro In vitro 4 unspecified role unspecified role prey prey Region 29-197 Region 29-197 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction