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Intrinsic selectivity in binding of matrix metalloproteinase‐7 to differently charged lipid membranes
Author(s) -
Ganguly Bratati,
Banerjee Jayati,
Elegbede Adekunle I.,
Klocke Donald J.,
Mallik Sanku,
Srivastava D.K.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.11.042
Subject(s) - membrane , cationic polymerization , chemistry , matrix metalloproteinase , selectivity , biophysics , static electricity , catalysis , biochemistry , polymer chemistry , biology , electrical engineering , engineering
We provide evidence that matrix metalloproteinase‐7 (MMP‐7) interacts with anionic, cationic and neutral lipid membranes, although it interacts strongest with anionic membranes. While the catalytic activity of the enzyme remains unaffected upon binding to neutral and negatively charged membranes, it is drastically impaired upon binding to the positively charged membranes. The structural data reveal that the origin of these features lies in the “bipolar” distribution of the electrostatic surface potentials on the crystallographic structure of MMP‐7.