1BIW

DESIGN AND SYNTHESIS OF CONFORMATIONALLY-CONSTRAINED MMP INHIBITORS

Summary for 1BIW

• Entry DOI: 10.2210/pdb1biw/pdb
• Descriptor: PROTEIN (STROMELYSIN-1 COMPLEX), ZINC ION, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: stromelysin, matrix metalloprotease, osteoarthritis, structure-based drug design, protein crystal structure, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix (Probable): P08254
• Total number of polymer chains: 2
• Total formula weight: 39750.69

Authors

Natchus, M.G.,Cheng, M.,Wahl, C.T.,Pikul, S.,Almstead, N.G.,Bradley, R.S.,Taiwo, Y.O.,Mieling, G.E.,Dunaway, C.M.,Snider, C.E.,McIver, J.M.,Barnett, B.L.,McPhail, S.J.,Anastasio, M.B.,De, B. (deposition date: 1998-06-19, release date: 1999-07-16, Last modification date: 2023-12-27)

Primary citation

Natchus, M.G.,Cheng, M.,Wahl, C.T.,Pikul, S.,Almstead, N.G.,Bradley, R.S.,Taiwo, Y.O.,Mieling, G.E.,Dunaway, C.M.,Snider, C.E.,McIver, J.M.,Barnett, B.L.,McPhail, S.J.,Anastasio, M.B.,De, B.
Design and synthesis of conformationally-constrained MMP inhibitors.
Bioorg.Med.Chem.Lett., 8:2077-2080, 1998

PubMed Abstract: A novel series of conformationally constrained matrix metalloprotease inhibitors was identified. The potencies observed for these inhibitors were highly dependent upon the substitution pattern on the caprolactam ring as well as the succinate moiety.

PubMed: 9873489
DOI: 10.1016/S0960-894X(98)00370-9

Experimental method

X-RAY DIFFRACTION (2.5 Å)