Structure of the protease domain of memapsin 2 (β-secretase) complexed with inhibitor
L Hong, G Koelsch, X Lin, S Wu, S Terzyan, AK Ghosh… - Science, 2000 - science.org
L Hong, G Koelsch, X Lin, S Wu, S Terzyan, AK Ghosh, XC Zhang, J Tang
Science, 2000•science.orgMemapsin 2 (β-secretase) is a membrane-associated aspartic protease involved in the
production of β-amyloid peptide in Alzheimer's disease and is a major target for drug design.
We determined the crystal structure of the protease domain of human memapsin 2
complexed to an eight-residue inhibitor at 1.9 angstrom resolution. The active site of
memapsin 2 is more open and less hydrophobic than that of other human aspartic
proteases. The subsite locations from S4 to S2′ are well defined. A kink of the inhibitor …
production of β-amyloid peptide in Alzheimer's disease and is a major target for drug design.
We determined the crystal structure of the protease domain of human memapsin 2
complexed to an eight-residue inhibitor at 1.9 angstrom resolution. The active site of
memapsin 2 is more open and less hydrophobic than that of other human aspartic
proteases. The subsite locations from S4 to S2′ are well defined. A kink of the inhibitor …
Memapsin 2 (β-secretase) is a membrane-associated aspartic protease involved in the production of β-amyloid peptide in Alzheimer's disease and is a major target for drug design. We determined the crystal structure of the protease domain of human memapsin 2 complexed to an eight-residue inhibitor at 1.9 angstrom resolution. The active site of memapsin 2 is more open and less hydrophobic than that of other human aspartic proteases. The subsite locations from S4 to S2′ are well defined. A kink of the inhibitor chain at P2′ and the change of chain direction of P3′ and P4′ may be mimicked to provide inhibitor selectivity.
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