2v00

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Revision as of 12:53, 23 January 2008 by OCA (talk | contribs) (New page: left|200px<br /><applet load="2v00" size="350" color="white" frame="true" align="right" spinBox="true" caption="2v00, resolution 1.55Å" /> '''X-RAY CRYSTAL STRUCT...)
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File:2v00.jpg


2v00, resolution 1.55Å

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X-RAY CRYSTAL STRUCTURE OF ENDOTHIAPEPSIN COMPLEXED WITH COMPOUND 1

OverviewOverview

Fragment-based lead generation was applied to find novel small-molecule, inhibitors of beta-secretase (BACE-1), a key target for the treatment of, Alzheimer's disease. Fragment hits coming from a 1D NMR screen were, characterized by BIAcore, and the most promising compounds were soaked, into protein crystals to help the rational design of more potent hit, analogues. Problems arising due to our inability to grow BACE-1 crystals, at the biologically relevant pH at which the screen was run were overcome, by using endothiapepsin as a surrogate aspartyl protease. Among others, we, identified 6-substituted isocytosines as a novel warhead against BACE-1, and the accompanying paper in this journal describes how these were, optimized to a lead series of nanomolar inhibitors.1.

About this StructureAbout this Structure

2V00 is a Single protein structure of sequence from Cryphonectria parasitica with , and as ligands. Active as Endothiapepsin, with EC number 3.4.23.22 Known structural/functional Sites: , , , , and . Full crystallographic information is available from OCA.

ReferenceReference

Discovery of a Novel Warhead against beta-Secretase through Fragment-Based Lead Generation., Geschwindner S, Olsson LL, Albert JS, Deinum J, Edwards PD, Beer T, Folmer RH, J Med Chem. 2007 Nov 29;50(24):5903-11. Epub 2007 Nov 7. PMID:17985861

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