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 http://mint.bio.uniroma2.it/mint anonymous-2014y-2 Collapse of the native structure by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase (NQO1) 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 2014 imex curation Lienhart W.D., Gudipati V., Uhl M.K., Binter A., Pulido S., Saf R., Zangger K., Gruber K., Macheroux P. FEBS J. (1742-464X) Only protein-protein interactions anonymous-2014t-4 Collapse of the native structure by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase (NQO1) 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 2014 imex curation Lienhart W.D., Gudipati V., Uhl M.K., Binter A., Pulido S., Saf R., Zangger K., Gruber K., Macheroux P. FEBS J. (1742-464X) Only protein-protein interactions anonymous-2014za-1 Collapse of the native structure by a single amino acid exchange in human NAD(P)H:quinone oxidoreductase (NQO1) in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined peter.macheroux@tugraz.at 2014 imex curation Lienhart W.D., Gudipati V., Uhl M.K., Binter A., Pulido S., Saf R., Zangger K., Gruber K., Macheroux P. FEBS J. (1742-464X) Only protein-protein interactions 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 1563260 n/a NQO1 P187S 1563263 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 false Stoichiometry: 2.0 direct interaction direct interaction false false false 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 1563260 n/a NQO1 P187S 1563263 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 false range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 2.0 direct interaction direct interaction false false false 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 1563261 n/a NQO1 P187S 1563263 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 false Stoichiometry: 2.0 direct interaction direct interaction false false false 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 1563261 n/a NQO1 1563263 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction false false false 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 1563262 n/a NQO1 P187S 1563263 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 false Stoichiometry: 2.0 direct interaction direct interaction false false false 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.