1fkn

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1fkn, resolution 1.90Å ()
Non-Standard Residues:
Activity: Memapsin 2, with EC number 3.4.23.46
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

Structure of Beta-Secretase Complexed with Inhibitor

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1fkn is a 4 chain structure with sequence from Homo sapiens. The July 2006 RCSB PDB Molecule of the Month feature on Amyloid-beta Precursor Protein by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_7. The July 2009 RCSB PDB Molecule of the Month feature on beta-Secretase by David Goodsell is 10.2210/rcsb_pdb/mom_2009_7. Full crystallographic information is available from OCA.

See Also

Reference

  • Hong L, Koelsch G, Lin X, Wu S, Terzyan S, Ghosh AK, Zhang XC, Tang J. Structure of the protease domain of memapsin 2 (beta-secretase) complexed with inhibitor. Science. 2000 Oct 6;290(5489):150-3. PMID:11021803

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