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 Structural insights into the calcium-dependent interaction between calbindin-D28K and caspase-3. Structural insights into the calcium-dependent interaction between calbindin-D28K and caspase-3. FEBS Lett. (0014-5793) 2012 Bobay BG., Stewart AL., Tucker AT., Thompson RJ., Varney KM., Cavanagh J. in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Bobay BG., Stewart AL., Tucker AT., Thompson RJ., Varney KM., Cavanagh J. FEBS Lett. (0014-5793) 2012 casp3_human Caspase-3 Apopain Cysteine protease CPP32 Protein Yama SREBP cleavage activity 1 CASP3 CPP32 protein protein human Homo sapiens Human MENTENSVDSKSIKNLEPKIIHGSESMDSGISLDNSYKMDYPEMGLCIIINNKNFHKSTGMTSRSGTDVDAANLRETFRNLKYEVRNKNDLTREEIVELMRDVSKEDHSKRSSFVCVLLSHGEEGIIFGTNGPVDLKKITNFFRGDRCRSLTGKPKLFIIQACRGTELDCGIETDSGVDDDMACHKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKQYADKLEFMHILTRVNRKVATEFESFSFDATFHAKKQIPCIVSMLTKELYFYH DIP protein P42574 original sequence version: 108 DIP protein P42574 original sequence version: 171 DIP protein P42574 original sequence version: 111 DIP protein P42574 original sequence version: 105 DIP protein P42574 original sequence version: 131 DIP protein P42574 original sequence version: 132 DIP protein P42574 original sequence version: 134 DIP protein P42574 original sequence version: 162 DIP protein P42574 original sequence version: 189 DIP protein P42574 original sequence version: 167 2F35CD3BCF7FF64A calb1_human Calbindin CALB1 CAB27 Calbindin D28 D-28K Vitamin D-dependent calcium-binding protein, avian-type protein protein human Homo sapiens Human MAESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELQQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQDLDINNITTYKKNIMALSDGGKLYRTDLALILCAGDN 8ED7A09BCC5FE5E4 calb1-casp3 1 Caspase-3 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Calbindin-D28K 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction f1 homomint mint ITC binding experiments (Fig. 1) indicate the following: (i) apo-calbindin-D28K does not bind caspase-3; (ii) 1Ca2+-loaded calbindin-D28K binds to caspase-3 with the binding most closely approximating a two-site model with an N-value (reaction stoichiometry) of 0.64 and 1.32; (iii) 2Ca2+-loaded calbindin-D28K binds to caspase-3 with the binding most closely approximating a two-site model (N-values of 1.28 and 1.90); (iv) 3Ca2+-loaded calbindin-D28K binds to caspase-3 with the binding moving from a two-site model more towards a one-site model (N-values of 1.60 and 0.53) ; (v) fully Ca2+-loaded calbindin-D28K binds to caspase-3 with the binding most closely 10 approximating a one-site model (N-value of 1.05). In each case the binding occurs with low micromolar affinity. These data are summarized in Table 1.