Summary
PDB 3EHX deposited: 2008-09-15 modified: 2009-05-19
Title Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor (R)-2-(biphenyl-4-ylsulfonamido)-4-methylpentanoic acid
Authors Calderone, V., Dragoni, E., Fragai, M., Jaiswal, R., Luchinat, C., Nativi, C.
Method X-RAY DIFFRACTION
Structure factors resolution 1.9 rfactor 0.16287 rfree 0.20083
DPI 0.41 theoretical min: 0.14
Related PDB Entries 1OS2 1OS9 1Y93 3EHY 3F15 3F16 3F17 3F18 3F19 3F1A
Citations

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

Cross References
Database source Identifier Description
PubMed 19275207 BCCHES
PubMed 12813751
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
3EHX/0 3EHX 0 monomer 0 1 6 1298