3I7G

MMP-13 in complex with a non zinc-chelating inhibitor

Summary for 3I7G

• Entry DOI: 10.2210/pdb3i7g/pdb
• Related: 3I7I
• Descriptor: Collagenase 3, ZINC ION, CALCIUM ION, ... (6 entities in total)
• Functional Keywords: protease, calcium, collagen degradation, disease mutation, disulfide bond, extracellular matrix, glycoprotein, hydrolase, metal-binding, metalloprotease, polymorphism, secreted, zinc, zymogen
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix (Probable): P45452
• Total number of polymer chains: 2
• Total formula weight: 39439.78

Authors

Farrow, N.A. (deposition date: 2009-07-08, release date: 2009-09-01, Last modification date: 2024-02-21)

Primary citation

Heim-Riether, A.,Taylor, S.J.,Liang, S.,Gao, D.A.,Xiong, Z.,Michael August, E.,Collins, B.K.,Farmer, B.T.,Haverty, K.,Hill-Drzewi, M.,Junker, H.D.,Mariana Margarit, S.,Moss, N.,Neumann, T.,Proudfoot, J.R.,Keenan, L.S.,Sekul, R.,Zhang, Q.,Li, J.,Farrow, N.A.
Improving potency and selectivity of a new class of non-Zn-chelating MMP-13 inhibitors.
Bioorg.Med.Chem.Lett., 19:5321-5324, 2009

PubMed Abstract: Discovery and optimization of potency and selectivity of a non-Zn-chelating MMP-13 inhibitor with the aid of protein co-crystal structural information is reported. This inhibitor was observed to have a binding mode distinct from previously published MMP-13 inhibitors. Potency and selectivity were improved by extending the hit structure out from the active site into the S1' pocket.

PubMed: 19692239
DOI: 10.1016/j.bmcl.2009.07.151

Experimental method

X-RAY DIFFRACTION (1.95 Å)