1.8-angstrom crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate prime-side inhibitor with a distinct selectivity profile

Betz M, Huxley P, Davies SJ, Mushtaq Y, Pieper M, Tschesche H, Bode W, GomisRuth FX (1997)
EUROPEAN JOURNAL OF BIOCHEMISTRY 247(1): 356-363.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
Matrix metalloproteinases (MMP) are zinc endopeptidases involved in tissue remodelling. They have been implicated in a series of pathologies, including cancer, arthritis, joint destruction and Alzheimer's disease. Human neutrophil collagenase represents one of the three interstitial collagenases that cleave triple-helical collagen of type I, II and III. Its catalytic domain (residues Phe79-Gly242) has been heterologously expressed in Escherichia coli and crystallized as a non-covalent complex with the hydroxamate inhibitor BB-1909, which has distinct selectivity against different MMP, in a crystal form. The crystal structure, refined to 0.18-nm resolution, shows that BB-1909 is a right-hand-side inhibitor that binds to the S-1'-S-3' subsites and coordinates to the catalytic Zn2+ in a bidentate manner via the hydroxyl and carbonyl oxygen atoms of the hydroxamate group in a similar manner to batimastat. The collagenase/BB-1909 complex is described in detail and compared with the collagenase/batimastat complex. These studies provide information on MMP specificity and thus may assist the development of more-selective MMP inhibitors.
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Zeitschriftentitel
EUROPEAN JOURNAL OF BIOCHEMISTRY
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247
Zeitschriftennummer
1
Seite
356-363
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eISSN
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Betz M, Huxley P, Davies SJ, et al. 1.8-angstrom crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate prime-side inhibitor with a distinct selectivity profile. EUROPEAN JOURNAL OF BIOCHEMISTRY. 1997;247(1):356-363.
Betz, M., Huxley, P., Davies, S. J., Mushtaq, Y., Pieper, M., Tschesche, H., Bode, W., et al. (1997). 1.8-angstrom crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate prime-side inhibitor with a distinct selectivity profile. EUROPEAN JOURNAL OF BIOCHEMISTRY, 247(1), 356-363. doi:10.1111/j.1432-1033.1997.00356.x
Betz, M., Huxley, P., Davies, S. J., Mushtaq, Y., Pieper, M., Tschesche, H., Bode, W., and GomisRuth, F. X. (1997). 1.8-angstrom crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate prime-side inhibitor with a distinct selectivity profile. EUROPEAN JOURNAL OF BIOCHEMISTRY 247, 356-363.
Betz, M., et al., 1997. 1.8-angstrom crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate prime-side inhibitor with a distinct selectivity profile. EUROPEAN JOURNAL OF BIOCHEMISTRY, 247(1), p 356-363.
M. Betz, et al., “1.8-angstrom crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate prime-side inhibitor with a distinct selectivity profile”, EUROPEAN JOURNAL OF BIOCHEMISTRY, vol. 247, 1997, pp. 356-363.
Betz, M., Huxley, P., Davies, S.J., Mushtaq, Y., Pieper, M., Tschesche, H., Bode, W., GomisRuth, F.X.: 1.8-angstrom crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate prime-side inhibitor with a distinct selectivity profile. EUROPEAN JOURNAL OF BIOCHEMISTRY. 247, 356-363 (1997).
Betz, M, Huxley, P, Davies, SJ, Mushtaq, Y, Pieper, M, Tschesche, Harald, Bode, W, and GomisRuth, FX. “1.8-angstrom crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate prime-side inhibitor with a distinct selectivity profile”. EUROPEAN JOURNAL OF BIOCHEMISTRY 247.1 (1997): 356-363.

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