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pubmed-article:11021803pubmed:abstractTextMemapsin 2 (beta-secretase) is a membrane-associated aspartic protease involved in the production of beta-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.lld:pubmed
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pubmed-article:11021803pubmed:articleTitleStructure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor.lld:pubmed
pubmed-article:11021803pubmed:affiliationProtein Studies Program and Crystallography Program, Oklahoma Medical Research Foundation, 825 NE 13th Street, Oklahoma City, OK 73104, USA.lld:pubmed
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