1fkn
STRUCTURE OF BETA-SECRETASE COMPLEXED WITH INHIBITOR
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| 1fkn, resolution 1.90Å () | |||||||||
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| Non-Standard Residues: | |||||||||
| Activity: | Memapsin 2, with EC number 3.4.23.46 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
OverviewOverview
Memapsin 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.
About this StructureAbout this Structure
1FKN is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1FKN with [Amyloid-beta Precursor Protein]. Full crystallographic information is available from OCA.
ReferenceReference
Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor., Hong L, Koelsch G, Lin X, Wu S, Terzyan S, Ghosh AK, Zhang XC, Tang J, Science. 2000 Oct 6;290(5489):150-3. PMID:11021803 Page seeded by OCA on Fri May 2 16:26:16 2008