DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature 2009 imex curation Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. DIP original experiment: DIP-249790X Nature 2009 IMEx The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature 2009 imex curation Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. DIP original experiment: DIP-249789X Nature 2009 IMEx The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature 2009 imex curation Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. DIP original experiment: DIP-249788X Nature 2009 IMEx The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature 2009 imex curation Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. DIP original experiment: DIP-249786X Nature 2009 IMEx The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature 2009 imex curation Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. 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 Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. DIP original experiment: DIP-249785X Nature 2009 IMEx The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature 2009 imex curation Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. Only protein-protein interactions in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. DIP original experiment: DIP-249791X Nature 2009 IMEx The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature 2009 imex curation Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. Only protein-protein interactions in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Scott FL., Stec B., Pop C., Dobaczewska MK., Lee JJ., Monosov E., Robinson H., Salvesen GS., Schwarzenbacher R., Riedl SJ. DIP original experiment: DIP-249787X Nature 2009 IMEx The Fas-FADD death domain complex structure unravels signalling by receptor clustering. fadd_human FAS-associated death domain protein FAS-associating death domain-containing protein Mediator of receptor induced toxicity FADD MORT1 GIG3 Growth-inhibiting gene 3 protein protein protein human Homo sapiens Human MDPFLVLLHSVSSSLSSSELTELKFLCLGRVGKRKLERVQSGLDLFSMLLEQNDLEPGHTELLRELLASLRRHDLLRRVDDFEAGAAAGAAPGEEDLCAAFNVICDNVGKDWRRLARQLKVSDTKIDSIEDRYPRNLTERVRESLRIWKNTEKENATVAHLVGALRSCQMNLVADLVQEVQQARDLQNRSGAMSPMSWNSDASTSEAS DIP protein Q13158 original sequence version: 155 DIP protein Q13158 original sequence version: 130 DIP protein Q13158 original sequence version: 110 DIP protein Q13158 original sequence version: 118 DIP protein Q13158 original sequence version: 141 DIP protein Q13158 original sequence version: 166 0E65E2F852E83507 p25445-1 Tumor necrosis factor receptor superfamily member 6 FAS APT1 FAS1 TNFRSF6 Apo-1 antigen Apoptosis-mediating surface antigen FAS FASLG receptor protein protein human Homo sapiens Human MLGIWTLLPLVLTSVARLSSKSVNAQVTDINSKGLELRKTVTTVETQNLEGLHHDGQFCHKPCPPGERKARDCTVNGDEPDCVPCQEGKEYTDKAHFSSKCRRCRLCDEGHGLEVEINCTRTQNTKCRCKPNFFCNSTVCEHCDPCTKCEHGIIKECTLTSNTKCKEEGSRSNLGWLCLLLLPIPLIVWVKRKEVQKTCRKHRKENQGSHESPTLNPETVAINLSDVDLSKYITTIAGVMTLSQVKGFVRKNGVNEAKIDEIKNDNVQDTAEQKVQLLRNWHQLHGKKEAYDTLIKDLKKANLCTLAEKIQTIILKDITSDSENSNFRNEIQSLV DIP protein P25445-1 original sequence version: 126 DIP protein P25445 original sequence version: 149 DIP protein P25445-1 original sequence version: 145 DIP protein P25445 original sequence version: 153 DIP protein P25445-1 original sequence version: 153 DIP protein P25445 original sequence version: 152 DIP protein P25445-1 original sequence version: 204 DIP protein P25445 original sequence version: 176 fas-fadd-2 2 8 unspecified role unspecified role prey prey Region 93-208 Region 93-208 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q13158:p.Leu172Glu L172E mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain L E This feature has been corrected as a result of our quality control procedures. The original label was 'L172E'. Wed May 02 16:27:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu172glu' Tue Jun 30 16:28:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Leu172Glu' ecolx Escherichia coli 9 unspecified role unspecified role bait bait Region 223-335 Region 223-335 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association fadd-fas-2 7 8 unspecified role unspecified role unspecified role unspecified role Region 93-208 Region 93-208 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 223-335 Region 223-335 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-3 5 8 unspecified role unspecified role unspecified role unspecified role Region 93-208 Region 93-208 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 223-335 Region 223-335 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-4 6 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 223-335 Region 223-335 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-5 3 8 unspecified role unspecified role bait bait Region 93-208 Region 93-208 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecolx Escherichia coli 9 unspecified role unspecified role prey prey Region 223-335 Region 223-335 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association fadd-fas-6 4 8 unspecified role unspecified role unspecified role unspecified role Region 93-208 Region 93-208 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 223-335 Region 223-335 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction fadd-fas-7 1 8 unspecified role unspecified role unspecified role unspecified role Region 93-208 Region 93-208 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role Region 223-335 Region 223-335 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction