Structure-Based Design of a Novel , Potent , and Selective Inhibitor for MMP-13 Utilizing NMR Spectroscopy and Computer-Aided Molecular Design

@inproceedings{ChenStructureBasedDO,
  title={Structure-Based Design of a Novel , Potent , and Selective Inhibitor for MMP-13 Utilizing NMR Spectroscopy and Computer-Aided Molecular Design},
  author={James M. Chen and Frances C. Nelson and Jeremy I. Levin and Dominick Mobilio and Franklin J. Moy and Ramaswamy Nilakantan and Arie Zask and Robert Powers}
}
The high-resolution NMR solution structure of the catalytic fragment of human collagenase-3 (MMP13) was used as a starting point for structure-based design of selective inhibitors for MMP-13. The major structural difference observed between the MMP structures is the relative size and shape of the S1 ′ pocket where this pocket is significantly longer for MMP-13, nearly reaching the surface of the protein. On the basis of the extended nature of the MMP-13 S1 ′ pocket an inhibitor potent and… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 32 extracted citations

Similar Papers

Loading similar papers…