Intrinsic selectivity in binding of matrix metalloproteinase-7 to differently charged lipid membranes.
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ABSTRACT:
SUBMITTER: Ganguly B
PROVIDER: S-EPMC2696809 | biostudies-literature | 2007 Dec
REPOSITORIES: biostudies-literature
Publications
Intrinsic selectivity in binding of matrix metalloproteinase-7 to differently charged lipid membranes.
Ganguly Bratati B Banerjee Jayati J Elegbede Adekunle I AI Klocke Donald J DJ Mallik Sanku S Srivastava D K DK
FEBS letters 20071126 29
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 ...[more]
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