Intrinsic selectivity in binding of matrix metalloproteinase-7 to differently charged lipid membranes.
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.
Ganguly
Bratati
B
Department of Chemistry, Biochemistry and Molecular Biology, North Dakota State University, Fargo, ND 58105, USA.
Banerjee
Jayati
J
Elegbede
Adekunle I
AI
Klocke
Donald J
DJ
Mallik
Sanku
S
Srivastava
D K
DK
D001665:Binding Sites; D002384:Catalysis; D006801:Humans; D020783:Matrix Metalloproteinase 7 / Q000737:chemistry / Q000378:metabolism*; D008563:Membrane Lipids / Q000378:metabolism*; D008958:Models, Molecular; D013050:Spectrometry, Fluorescence
D008563:Membrane Lipids; C060932:MMP7 protein, human; D020783:Matrix Metalloproteinase 7