Resonance assignments for stromelysin complexed with a β-sulfonyl hydroxamate inhibitor

Article
  • 53 Downloads

Abstract

The sequence specific 1H, 13C, and 15N resonance assignments for stromelysin, a Matrix metalloproteinase, are reported in this article. Almost 70% of assignable backbone and side-chain atoms were assigned in this highly dynamic protein.

Keywords

AUTOASSIGN NMR assignment Stromelysin-inhibitor complex 

Notes

Acknowledgments

We thank Donald E. Harper and Martha A. Warpehoski for synthesizing the β-sulfonyl hydroxamate inhibitor and Vincent P. Marshall, Gary L. Petzold and Roger A. Poorman for supplying stromelysin.

References

  1. Alcaraz LA, Banci L, Bertini I, Cantini F, Donaire A, Gonnelli L (2007) Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors. J Biol Inorg Chem 12:1197–1206CrossRefGoogle Scholar
  2. Arumugam S, Gao G, Patton BL, Semenchenko V, Brew K, Van Doren R (2003) Increased backbone mobility in beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3. J Mol Biol 327:719–734CrossRefGoogle Scholar
  3. Cawston TE (1996) Metalloproteinase inhibitors and the prevention of connective tissue breakdown. Pharmacol Ther 70:163–182CrossRefGoogle Scholar
  4. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293CrossRefGoogle Scholar
  5. Li Y, Zhang X, Melton R, Ganu V, And Gonnella NC (1998) Solution structure of the catalytic domain of human stromelysin-1 complexed to a potent, nonpeptidic inhibitor. Biochemistry 37:14048–14056CrossRefGoogle Scholar
  6. McCawley LJ, Matrisian LM (2000) Matrix metalloproteinases: multifunctional contributors to tumor progression. Mol Med Today 6:149–156CrossRefGoogle Scholar
  7. Moseley HNB, Monleon D, Montelione GT (2000) Automatic determination of protein backbone resonance assignments from triple-resonance NMR data. Methods Enzymo 339:91–108CrossRefGoogle Scholar
  8. Skiles JW, Gonnella NC, Jeng AY (2001) The design, structure, and therapeutic application of matrix metalloproteinase inhibitors. Curr Med Chem 8:425–474Google Scholar
  9. Stockman BJ, Waldon DJ, Gates JA, Scahill TA, Kloosterman DA, Mizsak SA, Jacobsen EJ, Belonga KL, Mitchell MA, Mao B, Petke JD, Goodman L, Powers EA, Ledbetter SR, Kaytes PS, Vogeli G, Marshall VP, Petzold GL, Poorman RA (1998) Solution structures of stromelysin complexed to thiadiazole inhibitors. Protein Sci 7:2281–2286CrossRefGoogle Scholar
  10. Warpehoski MA, Harper DE (1998) .beta.-sulfonyl hydroxamic acids. U. S. Patent 5,847,153Google Scholar
  11. Yuan P, Marshall VP, Petzold GL, Poorman RA, Stockman BJ (1999) Dynamics of stromelysin/inhibitor interactions studied by 15N NMR relaxation measurements: comparison of ligand binding to the S1–S3 and S′1–S′3 subsites. J Biomol NMR 15:55–64CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2009

Authors and Affiliations

  1. 1.Exploratory Medicinal SciencesPfizer Global Research & DevelopmentGrotonUSA
  2. 2.Department of ChemistryAdelphi UniversityGarden CityUSA

Personalised recommendations