MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Collapse of the native structure by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase (NQO1). Collapse of the native structure by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase (NQO1). FEBS J. (1742-464X) 2014 imex curation Lienhart W.D., Gudipati V., Uhl M.K., Binter A., Pulido S., Saf R., Zangger K., Gruber K., Macheroux P. peter.macheroux@tugraz.at 18-Sep-2014: Contacted by IntAct-Help. 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 peter.macheroux@tugraz.at Accepted 2014-AUG-06 by MARTA 2014 imex curation Collapse of the native structure by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase (NQO1). Collapse of the native structure by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase (NQO1). FEBS J. (1742-464X) 2014 imex curation Lienhart W.D., Gudipati V., Uhl M.K., Binter A., Pulido S., Saf R., Zangger K., Gruber K., Macheroux P. peter.macheroux@tugraz.at 18-Sep-2014: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined peter.macheroux@tugraz.at Accepted 2014-AUG-06 by MARTA 2014 imex curation Collapse of the native structure by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase (NQO1). Collapse of the native structure by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase (NQO1). FEBS J. (1742-464X) 2014 imex curation Lienhart W.D., Gudipati V., Uhl M.K., Binter A., Pulido S., Saf R., Zangger K., Gruber K., Macheroux P. peter.macheroux@tugraz.at 18-Sep-2014: Contacted by IntAct-Help. 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 peter.macheroux@tugraz.at Accepted 2014-AUG-06 by MARTA 2014 imex curation nqo1_human NAD(P)H dehydrogenase [quinone] 1 NQO1 DIA4 NMOR1 Azoreductase DT-diaphorase Menadione reductase NAD(P)H:quinone oxidoreductase 1 Phylloquinone reductase Quinone reductase 1 protein protein human Homo sapiens Human MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVFIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKKEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK nqo1-2 2 NQO1 P187S 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P15559:p.Pro187Ser mutation mutation certain certain sequence position certain certain certain sequence position certain P S Wed May 02 15:44:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro187ser' Tue Jun 30 16:54:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro187Ser' direct interaction direct interaction F3 The calculated size of NQO1 (61 kDa) agrees well with the theoretical size of NQO1 dimers (62 kDa), on the other hand the calculated size of NQO1 P187S (78.33 kDa) suggests that the hydrodynamic radius is larger compared to that of NQO1. nqo1-2 1 NQO1 P187S 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P15559:p.Pro187Ser mutation mutation certain certain sequence position certain certain certain sequence position certain P S Wed May 02 17:40:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro187ser' Tue Jun 30 19:04:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro187Ser' direct interaction direct interaction sf2 st1 These crystals diffracted to 2.7 Å and revealed a structural topology (Fig. 2A) virtually identical to the NQO1 crystal structure [15, 16] with a root-mean-square-deviation of 0.33 Å for 249 Cα atoms. nqo1-2 1 NQO1 P187S 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P15559:p.Pro187Ser mutation mutation certain certain sequence position certain certain certain sequence position certain P S Wed May 02 17:27:44 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro187ser' Tue Jun 30 16:46:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro187Ser' range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction sf2 st1 These crystals diffracted to 2.7 Å and revealed a structural topology (Fig. 2A) virtually identical to the NQO1 crystal structure [15, 16] with a root-mean-square-deviation of 0.33 Å for 249 Cα atoms. nqo1-2 3 NQO1 P187S 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified P15559:p.Pro187Ser mutation mutation certain certain sequence position certain certain certain sequence position certain P S Wed May 02 16:44:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro187ser' Tue Jun 30 19:20:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro187Ser' direct interaction direct interaction sf4 Analytical size exclusion chromatograms of purified NQO1 (continuous line) and NQO1 P187S (Dashed line) obtained using a using a Superdex 200 (10/300) analytical column. The calculated molecular mass of NQO1 (61.3 kDa) and NQO1 P187S (78.33 kDa) indicate that both the proteins exist in dimeric forms. The lower elution volume observed for NQO1 P187S indicates that deviation from the globular structure adopted by NQO1, thus supporting our NMR data that the P187S variant exhibits a more disordered structure compared to that of NQO1 nqo1-2 3 NQO1 4 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction sf4 Analytical size exclusion chromatograms of purified NQO1 (continuous line) and NQO1 P187S (Dashed line) obtained using a using a Superdex 200 (10/300) analytical column. The calculated molecular mass of NQO1 (61.3 kDa) and NQO1 P187S (78.33 kDa) indicate that both the proteins exist in dimeric forms. The lower elution volume observed for NQO1 P187S indicates that deviation from the globular structure adopted by NQO1, thus supporting our NMR data that the P187S variant exhibits a more disordered structure compared to that of NQO1