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Solution structure of wild-type human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor

  • NMR Structure Note
  • Published:
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Fig. 1
Fig. 2
Fig. 3

Notes

  1. The wild type human sequence (methionine plus F100 to G263) is used here, the F171D mutation (in the context of methionine plus G106 to G263) for 1YCM, and the E219A inactivating mutation (in the context of F100 to G263) for 2POJ.

  2. The respective buffer conditions are: here—50 mM deuterated MES, 20 mM CaCl2, 50 μM ZnCl2, 100 mM NaCl, 200 μM NaN3, pH 6.0; 1YCM—10 mM deuterated Tris, 5 mM CaCl2, 100 μM ZnCl2, 300 mM NaCl, pH 7.2; 2POJ—20 mM imidazole, 10 mM CaCl2, 20 mM ZnCl2, pH 6.6.

Abbreviations

3D:

Three dimensional

4D:

Four dimensional

DSV:

N-(Dibenzo[b,d]thiophene-3-sulfonyl) valine

IPAP:

In-phase antiphase (used for measuring H–N residual dipolar couplings)

MMP:

Matrix metalloproteinase

NNGH:

n-Isobutyl-N-[4-methoxyphenyl-sulfonyl]glycyl hydroxamic acid

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Acknowledgements

We thank Charles Schwieters for assistance with X-PLOR calculations. We thank Ad Bax for pulse sequences and advice on spectroscopy.

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Author notes

  1. Brian Dwyer

    Present address: Novartis, 400 Technology Square, Cambridge, MA, 02139, USA

  2. Scott Wolfrom

    Present address: Protein Engineering and Chemistry, Adnexus Therapeutics, Waltham, MA, 02453, USA

Authors and Affiliations

  1. Structural Biology and Computational Chemistry, Chemical and Screening Sciences, Wyeth Research, 87 CambridgePark Drive, Cambridge, MA, 02140, USA

    Michelle A. Markus, Brian Dwyer, Scott Wolfrom, Karl Malakian, James Wilhelm & Désirée H. H. Tsao

  2. Medicinal Chemistry, Chemical and Screening Sciences, Wyeth Research, 87 CambridgePark Drive, Cambridge, MA, 02140, USA

    Jianchang Li & Wei Li

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  1. Michelle A. Markus
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Correspondence to Michelle A. Markus.

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Markus, M.A., Dwyer, B., Wolfrom, S. et al. Solution structure of wild-type human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor. J Biomol NMR 41, 55–60 (2008). https://doi.org/10.1007/s10858-008-9236-4

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