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 The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. The Rac-RhoGDI complex and the structural basis for the regulation of Rho proteins by RhoGDI. Nat. Struct. Biol. (1072-8368) 2000 Scheffzek K., Stephan I., Jensen ON., Illenberger D., Gierschik P. no klaus@mpimf-heidelberg.mpg.de in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Scheffzek K., Stephan I., Jensen ON., Illenberger D., Gierschik P. no klaus@mpimf-heidelberg.mpg.de Nat. Struct. Biol. (1072-8368) 2000 rac2_human Ras-related C3 botulinum toxin substrate 2 p21-Rac2 Small G protein GX RAC2 protein protein human Homo sapiens Human MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASYENVRAKWFPEVRHHCPSTPIILVGTKLDLRDDKDTIEKLKEKKLAPITYPQGLALAKEIDSVKYLECSALTQRGLKTVFDEAIRAVLCPQPTRQQKRACSLL DIP protein P15153 original sequence version: 154 DIP protein P15153 original sequence version: 153 DIP protein P15153 original sequence version: 123 2A1F1266B07C3210 gdir2_human Rho GDP-dissociation inhibitor 2 GDIA2 GDID4 RAP1GN1 Ly-GDI Rho-GDI beta ARHGDIB protein protein human Homo sapiens Human MTEKAPEPHVEEDDDDELDSKLNYKPPPQKSLKELQEMDKDDESLIKYKKTLLGDGPVVTDPKAPNVVVTRLTLVCESAPGPITMDLTGDLEALKKETIVLKEGSEYRVKIHFKVNRDIVSGLKYVQHTYRTGVKVDKATFMVGSYGPRPEEYEFLTPVEEAPKGMLARGTYHNKSFFTDDDKQDHLSWEWNLSIKKEWTE DIP protein P52566 original sequence version: 104 F1E840134F643E5F arhgdib-rac2 1 3 unspecified role unspecified role unspecified role unspecified role purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain N-TERM (ISOPRENYL BINDING SITE) range MINT-1616384: original sequence: 1-74 : MTEKAPEPHVEEDDDDELDSKLNYKPPPQKSLKELQEMDKDDESLIKYKKTLLGDGPVVTDPKAPNVVVTRLT Stoichiometry: 1.0 2 unspecified role unspecified role unspecified role unspecified role purified purified binding site binding region binding-associated region binding region deletion analysis deletion analysis certain certain sequence position certain c-terminal c-terminal position c-term carboxy-terminus c-terminus c-term c-terminus carboxy-terminus c-terminal range MINT-1616391: original sequence: 161-192 : TQRGLKTVFDEAIRAVLCPQPTRQQKRACSL Stoichiometry: 1.0 direct interaction direct interaction An inner segment of LyN forms a helical hairpin that contacts mainly the switch regions of Rac2. homomint mint arhgdib-rac2-1 1 3 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 2 nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence predetermined predetermined participant predetermined unspecified role unspecified role unspecified role unspecified role purified purified tagged molecule tag tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 1.0 direct interaction direct interaction In the xray complex 1ds6, P15153 is chain A and P52566 is chain B Resolution 2.350 homomint mint