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 Crystal structure of phospholipase PA2-Vb, a protease-activated receptor agonist from the Trimeresurus stejnegeri snake venom. Crystal structure of phospholipase PA2-Vb, a protease-activated receptor agonist from the Trimeresurus stejnegeri snake venom. FEBS Lett. (0014-5793) 2014 imex curation Zeng F., Zhang W., Xue N., Teng M., Li X., Shen B. sachem@ustc.edu.cn 26-Feb-2015: 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 Zeng F., Zhang W., Xue N., Teng M., Li X., Shen B. sachem@ustc.edu.cn Accepted 2015-FEB-09 by LUANA FEBS Lett. (0014-5793) 2014 Only protein-protein interactions imex curation Crystal structure of phospholipase PA2-Vb, a protease-activated receptor agonist from the Trimeresurus stejnegeri snake venom. Crystal structure of phospholipase PA2-Vb, a protease-activated receptor agonist from the Trimeresurus stejnegeri snake venom. FEBS Lett. (0014-5793) 2014 imex curation Zeng F., Zhang W., Xue N., Teng M., Li X., Shen B. sachem@ustc.edu.cn 26-Feb-2015: 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 Zeng F., Zhang W., Xue N., Teng M., Li X., Shen B. sachem@ustc.edu.cn Accepted 2015-FEB-09 by LUANA FEBS Lett. (0014-5793) 2014 Only protein-protein interactions imex curation pa2a5_trist Acidic phospholipase A2 5 PLA2-V Phosphatidylcholine 2-acylhydrolase protein protein trist Trimeresurus stejnegeri Viridovipera stejnegeri NLMQFELLIMKVAGRSGIVWYSDYGCFCGKGGHGRPQDATDRCCFVHDCCYGKVTECDPKMDFYRYSSNNGDIVCEANNPCTKEICECDKAAAICFRDNKDTYDNKYWNIPMEGCQEESEPC 8B20A1D3907EB522 pa2a5-1 2 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f1c The results of Superdex 200 chromatography indicate that PA2- Vb is predominantly in a monomer in solution. But a significant homodimer peak was also observed (Fig. 1c). The SDS–PAGEanalysis of PA2-Vb under non-reducing conditions showed a single band for the monomer (insertion of Fig. 1c).This indicates that the homodimer in the solution is not formed by disulfide bond pa2a5-1 1 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f7 t1