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-2014v-1 Development of highly potent anti-angiogenic VEGF8-109 heterodimer by directed blocking of its VEGFR-2 binding site in vitro In vitro comigration in sds comigration in sds page comigration in sds weight by comassie molecular weight estimation by coomasie staining weight by comassie sajedi_r@modares.ac.ir 2014 imex curation Ghavamipour F., Shirin Shahangian S., Sajedi R.H., Shahriar Arab S., Mansouri K., Aghamaali M.R. FEBS J. (1742-464X) Only protein-protein interactions vegfa_human Vascular endothelial growth factor A Vascular permeability factor VEGFA VEGF protein protein human Homo sapiens Human MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPHPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR vegfa-vegfa 1563064 n/a M-VEGF 1563065 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified strep tag strep tag strep tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a WT-VEGF 1563065 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false Stoichiometry: 2.0 direct interaction direct interaction false false false f5 We appraised whether the refolded constructs form dimer by reducing and non-reducing SDS-PAGE. The refolded WT VEGF, HD-VEGF and M-VEGF revealed 28 kDa bands at the expected position of dimeric VEGF RBD under non-reducing condition, whereas the same sample appeared at the position corresponded to monomer in reducing conditions (data not shown). These analyses confirmed that the refolded proteins are disulfide-linked dimer. M-VEGF= Two most important segments of VEGF for KDR binding, including 41DEIEYI46 and 81 MRIKPHQ87, were replaced with segments 166GEGDEILT 173 and 42HGLRPSVA46 from two different x-ray crystallized proteins (PDB ID: 1XRH and 1SGL respectively).