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-2014x-1 L-Asp is a useful tool in the purification of the ionotropic glutamate receptor A2 ligand-binding domain in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined jsk@sund.ku.dk 2014 imex curation Krintel C., Frydenvang K., Ceravalls de Rabassa A., Kaern A.M., Gajhede M., Pickering D.S., Kastrup J.S. FEBS J. (1742-464X) Only protein-protein interactions gria2_rat Glutamate receptor 2 Gria2 Glur2 GluR-B GluR-K2 Glutamate receptor ionotropic, AMPA 2 AMPA-selective glutamate receptor 2 protein protein rat Rattus norvegicus (Rat) Rat MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINNDKKDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTATIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTLTELPSGNDTSGLENKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEDGRETQSSESTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKEKTSALSLSNVAGVFYILVGGLGLAMLVALIEFCYKSRAEAKRMKVAKNPQNINPSSSQNSQNFATYKEGYNVYGIESVKI gria2-2 1530444 n/a GluA2 1530445 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified binding region binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false Stoichiometry: 2.0 direct interaction direct interaction false false false t1 f4a To evaluate GluA2 LBD purified in the presence of L-Asp, we crystallized and solved the structure of GluA2 LBD in the presence of 7.5 mM, 50 mM and 250 mM L-Asp, respectively. The structures were determined to 1.9 Å, 1.5 Å and 1.8 Å resolution, respectively. GluA2 LBD with 7.5 mM L-Asp crystallized as a dimer with two subunits in the asymmetric unit of the crystal (Figure 4A).