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.
Department of Chemistry, Biochemistry and Molecular Biology, North Dakota State University, Fargo, ND 58105, USA.
Bratati
B
Ganguly
Jayati
J
Banerjee
Adekunle I
AI
Elegbede
Donald J
DJ
Klocke
Sanku
S
Mallik
D K
DK
Srivastava
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