Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:3.2
Classification:hydrolase/hydrolase inhibitor
Release Date:2017-07-12
Deposition Date:2017-02-21
Revision Date:2017-07-26
Molecular Weight:101515.55
Macromolecule Type:Protein
Residue Count:860
Atom Site Count:6833
DOI:10.2210/pdb5uwn/pdb
Abstract:
We describe the use of comparative structural analysis and structure-guided molecular design to develop potent and selective inhibitors (10d and (S)-17b) of matrix metalloproteinase 13 (MMP-13). We applied a three-step process, starting with a comparative analysis of the X-ray crystallographic structure of compound 5 in complex with MMP-13 with published structures of known MMP-13·inhibitor complexes followed by molecular design and synthesis of potent but nonselective zinc-chelating MMP inhibitors (e.g., 10a and 10b). After demonstrating that the pharmacophores of the chelating inhibitors (S)-10a, (R)-10a, and 10b were binding within the MMP-13 active site, the Zn
Resolution:3.2
Classification:hydrolase/hydrolase inhibitor
Release Date:2017-07-12
Deposition Date:2017-02-21
Revision Date:2017-07-26
Molecular Weight:101515.55
Macromolecule Type:Protein
Residue Count:860
Atom Site Count:6833
DOI:10.2210/pdb5uwn/pdb
Abstract:
We describe the use of comparative structural analysis and structure-guided molecular design to develop potent and selective inhibitors (10d and (S)-17b) of matrix metalloproteinase 13 (MMP-13). We applied a three-step process, starting with a comparative analysis of the X-ray crystallographic structure of compound 5 in complex with MMP-13 with published structures of known MMP-13·inhibitor complexes followed by molecular design and synthesis of potent but nonselective zinc-chelating MMP inhibitors (e.g., 10a and 10b). After demonstrating that the pharmacophores of the chelating inhibitors (S)-10a, (R)-10a, and 10b were binding within the MMP-13 active site, the Zn
| Date made available | 2017 |
|---|---|
| Publisher | RCSB-PDB |