Assignments for the main-chain nuclear magnetic resonances and delineation of the secondary structure of the catalytic domain of human stromelysin-1 as obtained from triple-resonance 3D NMR experiments

S. R. Van Doren, A. V. Kurochkin, Q. Z. Ye, Qizhuang Ye, D. J. Hupe, E. R P Zuiderweg

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Abstract

We report the NMR assignments for the main-chain 13C, 15N, and 1H resonances (1HN, 1H(α), 15N(α), 13C(α), 13CO) for the 19.5-kDa catalytic domain of human stromelysin-1, a zinc endoproteinase thought to be involved in pathologic tissue degradation. The assignments were predominantly obtained from triple-resonance three-dimensional NMR experiments using double-labeled (15N/13C) samples. The secondary structure of the molecule was determined from analysis of 3D 15N-resolved NOESY experiments. It was found to consist of a five-stranded mixed β-sheet with four parallel and one antiparallel strand and three helices. The topological arrangement of the secondary structure elements of stromelysin catalytic domain is remarkably similar to that found for astacin, a Zn proteinase for which the tertiary structure was recently determined from X-ray diffraction data [Bode et al. (1992) Nature 358, 164-167].

Original languageEnglish (US)
Pages (from-to)13109-13122
Number of pages14
JournalBiochemistry
Volume32
Issue number48
DOIs
StatePublished - 1993
Externally publishedYes

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Matrix Metalloproteinase 3
Catalytic Domain
Magnetic Resonance Spectroscopy
Nuclear magnetic resonance
X-Ray Diffraction
Zinc
Peptide Hydrolases
Experiments
Tissue
X ray diffraction
Degradation
Molecules
astacin

ASJC Scopus subject areas

  • Biochemistry

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Assignments for the main-chain nuclear magnetic resonances and delineation of the secondary structure of the catalytic domain of human stromelysin-1 as obtained from triple-resonance 3D NMR experiments. / Van Doren, S. R.; Kurochkin, A. V.; Ye, Q. Z.; Ye, Qizhuang; Hupe, D. J.; Zuiderweg, E. R P.

In: Biochemistry, Vol. 32, No. 48, 1993, p. 13109-13122.

Research output: Contribution to journalArticle

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abstract = "We report the NMR assignments for the main-chain 13C, 15N, and 1H resonances (1HN, 1H(α), 15N(α), 13C(α), 13CO) for the 19.5-kDa catalytic domain of human stromelysin-1, a zinc endoproteinase thought to be involved in pathologic tissue degradation. The assignments were predominantly obtained from triple-resonance three-dimensional NMR experiments using double-labeled (15N/13C) samples. The secondary structure of the molecule was determined from analysis of 3D 15N-resolved NOESY experiments. It was found to consist of a five-stranded mixed β-sheet with four parallel and one antiparallel strand and three helices. The topological arrangement of the secondary structure elements of stromelysin catalytic domain is remarkably similar to that found for astacin, a Zn proteinase for which the tertiary structure was recently determined from X-ray diffraction data [Bode et al. (1992) Nature 358, 164-167].",
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T1 - Assignments for the main-chain nuclear magnetic resonances and delineation of the secondary structure of the catalytic domain of human stromelysin-1 as obtained from triple-resonance 3D NMR experiments

AU - Van Doren, S. R.

AU - Kurochkin, A. V.

AU - Ye, Q. Z.

AU - Ye, Qizhuang

AU - Hupe, D. J.

AU - Zuiderweg, E. R P

PY - 1993

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N2 - We report the NMR assignments for the main-chain 13C, 15N, and 1H resonances (1HN, 1H(α), 15N(α), 13C(α), 13CO) for the 19.5-kDa catalytic domain of human stromelysin-1, a zinc endoproteinase thought to be involved in pathologic tissue degradation. The assignments were predominantly obtained from triple-resonance three-dimensional NMR experiments using double-labeled (15N/13C) samples. The secondary structure of the molecule was determined from analysis of 3D 15N-resolved NOESY experiments. It was found to consist of a five-stranded mixed β-sheet with four parallel and one antiparallel strand and three helices. The topological arrangement of the secondary structure elements of stromelysin catalytic domain is remarkably similar to that found for astacin, a Zn proteinase for which the tertiary structure was recently determined from X-ray diffraction data [Bode et al. (1992) Nature 358, 164-167].

AB - We report the NMR assignments for the main-chain 13C, 15N, and 1H resonances (1HN, 1H(α), 15N(α), 13C(α), 13CO) for the 19.5-kDa catalytic domain of human stromelysin-1, a zinc endoproteinase thought to be involved in pathologic tissue degradation. The assignments were predominantly obtained from triple-resonance three-dimensional NMR experiments using double-labeled (15N/13C) samples. The secondary structure of the molecule was determined from analysis of 3D 15N-resolved NOESY experiments. It was found to consist of a five-stranded mixed β-sheet with four parallel and one antiparallel strand and three helices. The topological arrangement of the secondary structure elements of stromelysin catalytic domain is remarkably similar to that found for astacin, a Zn proteinase for which the tertiary structure was recently determined from X-ray diffraction data [Bode et al. (1992) Nature 358, 164-167].

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