(Q27765120)

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High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3

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High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3 (English)

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author name string

F W Muskett

1

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T A Frenkiel

2

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J Feeney

3

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R B Freedman

4

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M D Carr

5

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R A Williamson

6

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language of work or name

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publication date

21 August 1998

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Journal of Biological Chemistry

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273

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34

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21736-43

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The matrix metalloproteinases and their natural inhibitors: prospects for treating degenerative tissue diseases

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Cloning of the cDNA encoding human tissue inhibitor of metalloproteinases-3 (TIMP-3) and mapping of the TIMP3 gene to chromosome 22

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Tissue inhibitors of matrix metalloendopeptidases

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The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3.

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The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity

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Solution structure of the active domain of tissue inhibitor of metalloproteinases-2. A new member of the OB fold protein family

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Chemically and conformationally authentic active domain of human tissue inhibitor of metalloproteinases-2 refolded from bacterial inclusion bodies.

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Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1

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Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation

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Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)

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The solution structure of eglin c based on measurements of many NOEs and coupling constants and its comparison with X‐ray structures

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Identifiers

10.1074/JBC.273.34.21736

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