MMP-TIMP interaction depends on residue 2 in TIMP-4

Stratmann B, Farr M, Tschesche H (2001)
FEBS LETTERS 507(3): 285-287.

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Abstract
Extracellular matrix remodeling and degradation are of great importance in both physiological and pathological: situations. Matrix metalloproteinases (MMPs) and their, natural occurring inhibitors - tissue inhibitors of metalloproteinases (TIMPs) - are involved in matrix turnover. Among the TIMP's there is only little specificity for inhibiting individual MMPs. In this report we describe the mutational analysis of the interaction of human TIMP-4 with several MMPs. The effects of different substitutions of residue 2 (Ser(2)) in the inhibitory domain of TIMP-4 were determined by kinetic measurements. Size, charge and polarity of residue 2 in the TIMP structure are key factors in MMP inhibition. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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Stratmann B, Farr M, Tschesche H. MMP-TIMP interaction depends on residue 2 in TIMP-4. FEBS LETTERS. 2001;507(3):285-287.
Stratmann, B., Farr, M., & Tschesche, H. (2001). MMP-TIMP interaction depends on residue 2 in TIMP-4. FEBS LETTERS, 507(3), 285-287.
Stratmann, B., Farr, M., and Tschesche, H. (2001). MMP-TIMP interaction depends on residue 2 in TIMP-4. FEBS LETTERS 507, 285-287.
Stratmann, B., Farr, M., & Tschesche, H., 2001. MMP-TIMP interaction depends on residue 2 in TIMP-4. FEBS LETTERS, 507(3), p 285-287.
B. Stratmann, M. Farr, and H. Tschesche, “MMP-TIMP interaction depends on residue 2 in TIMP-4”, FEBS LETTERS, vol. 507, 2001, pp. 285-287.
Stratmann, B., Farr, M., Tschesche, H.: MMP-TIMP interaction depends on residue 2 in TIMP-4. FEBS LETTERS. 507, 285-287 (2001).
Stratmann, B, Farr, M, and Tschesche, Harald. “MMP-TIMP interaction depends on residue 2 in TIMP-4”. FEBS LETTERS 507.3 (2001): 285-287.
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