||3EHX deposited: 2008-09-15 modified: 2009-05-19
||Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor (R)-2-(biphenyl-4-ylsulfonamido)-4-methylpentanoic acid
||Calderone, V., Dragoni, E., Fragai, M., Jaiswal, R., Luchinat, C., Nativi, C.
||resolution 1.9 rfactor 0.16287 rfree 0.20083
theoretical min: 0.14
|Related PDB Entries
The design and synthesis of biotin chain-terminated inhibitors (BTI) showing high affinity for matrix metalloproteinases (MMPs) on one side and high affinity for avidin through the biotinylated tag on the other are reported. The affinity of the designed BTI toward five different MMPs has been evaluated and the simultaneous formation of a highly stable ternary system Avidin-BTI-MMP clearly assessed. This system will permit the development of new approaches to detect, quantify, or collect MMPs in biological samples, with potential applications in vivo.
Bioconjug.Chem. 2009 Apr; 20(4):719-727 doi:10.1021/bc8003827
Angew.Chem.Int.Ed.Engl. 2003 Jun; 42(23):2673-2676 doi:10.1002/anie.200350957