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-2014j-1 Conformational modulation and hydrodynamic radii of CP12 protein and its complexes probed by Fluorescence Correlation Spectroscopy in vitro In vitro fcs fluorescence correlation spectroscopy FCS FCS fcs tag fluorescence tag visualisation by fluorescence tag fluorescence satish.moparthi@fresnel.fr 2014 imex curation Moparthi S.B., Thieulin-Pardo G., Mansuelle P., Rigneault H., Gontero B., Wenger J. FEBS J. (1742-464X) Only protein-protein interactions kppr_chlre Phosphoribulokinase, chloroplastic PRKA Phosphopentokinase protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii MAFTMRAPAPRATAQSRVTANRARRSLVVRADKDKTVVIGLAADSGCGKSTFMRRMTSIFGGVPKPPAGGNPDSNTLISDMTTVICLDDYHCLDRNGRKVKGVTALAPEAQNFDLMYNQVKALKEGKSVDKPIYNHVSGLIDAPEKIESPPILVIEGLHPFYDKRVAELLDFKIYLDISDDIKFAWKIQRDMAERGHSLESIKSSIAARKPDFDAYIDPQKKDADMIIQVLPTQLVPDDKGQYLRVRLIMKEGSKMFDPVYLFDEGSTISWIPCGRKLTCSFPGIKMFYGPDTWYGQEVSVLEMDGQFDKLEELIYVESHLSNTSAKFYGEITQQMLKNSGFPGSNNGTGLFQTIVGLKVREVYERIVKKDVVPV cp12_chlre Calvin cycle protein CP12, chloroplastic CP12 CP12 domain-containing protein Chloroplast protein 12 CHLREDRAFT_148487 protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii MMLTKSVVISRPAVRPVSTRRAVVVRASGQPAVDLNKKVQDAVKEAEDACAKGTSADCAVAWDTVEELSAAVSHKKDAVKADVTLTDPLEAFCKDAPDADECRVYED g3pa_chlre Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic GAPA NADP-dependent glyceraldehydephosphate dehydrogenase subunit A protein protein chlre Chlamydomonas reinhardtii Chlamydomonas smithii MAAMMQKSAFTGSAVSSKSGVRAKAARAVVDVRAEKKIRVAINGFGRIGRNFLRCWHGRQNTLLDVVAINDSGGVKQASHLLKYDSTLGTFAADVKIVDDSHISVDGKQIKIVSSRDPLQLPWKEMNIDLVIEGTGVFIDKVGAGKHIQAGASKVLITAPAKDKDIPTFVVGVNEGDYKHEYPIISNASCTTNCLAPFVKVLEQKFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTTTGAAKAVSLVLPSLKGKLNGIALRVPTPTVSVVDLVVQVEKKTFAEEVNAAFREAANGPMKGVLHVEDAPLVSIDFKCTDQSTSIDASLTMVMGDDMVKVVAWYDNEWGYSQRVVDLAEVTAKKWVA cp12-prka 1539573 n/a PRK 1539574 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified n/a CP12 1539575 tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component purified purified tag fluorophore fluorophore undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false A6Q0K5:p.Pro31Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false direct interaction direct interaction false false false T1 T2 F2 F3 F4 Our results showed that the disruption of the N-terminal disulfide bridge on CP12 affects the formation of the CP12C31S-PRK complex, while it has no effect on the CP12C31S-GAPDH complex. On the other hand, we observed the opposite effect with the mutant CP12C75S affected at the C-terminal disulfide bridge that forms a complex with PRK but not with GAPDH. cp12-prka-1 1539573 n/a CP12 1539575 tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component purified purified A6Q0K5:p.Lys75Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false tag fluorophore fluorophore undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false n/a GAPDH 1539576 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false T1 T2 F2 F3 F4 Our results showed that the disruption of the N-terminal disulfide bridge on CP12 affects the formation of the CP12C31S-PRK complex, while it has no effect on the CP12C31S-GAPDH complex. On the other hand, we observed the opposite effect with the mutant CP12C75S affected at the C-terminal disulfide bridge that forms a complex with PRK but not with GAPDH. cp12-gapa-1 1539573 n/a PRK 1539574 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified n/a CP12 1539575 tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role neutral component neutral component purified purified tag fluorophore fluorophore undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false A6Q0K5:p.Lys75Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false n/a GAPDH 1539576 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association false false false T1 T2 F2 F3 F4 Our results showed that the disruption of the N-terminal disulfide bridge on CP12 affects the formation of the CP12C31S-PRK complex, while it has no effect on the CP12C31S-GAPDH complex. On the other hand, we observed the opposite effect with the mutant CP12C75S affected at the C-terminal disulfide bridge that forms a complex with PRK but not with GAPDH.