3MSK

Fragment Based Discovery and Optimisation of BACE-1 Inhibitors

Summary for 3MSK

• Entry DOI: 10.2210/pdb3msk/pdb
• Related: 3MSJ 3MSL 3MSM
• Descriptor: Beta-secretase 1, IODIDE ION, GLYCEROL, ... (5 entities in total)
• Functional Keywords: protease, alzheimer's disease, aspartic protease, aspartyl protease, base, beta-secretase, glycoprotein, hydrolase, memapsin 2, amyloid precursor protein secretases, aspartic endopeptidases, fragment-based drug design, fluorescence polarisation, transmembrane, zymogen, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P56817
• Total number of polymer chains: 1
• Total formula weight: 46002.83

Authors

Smith, M.A.,Madden, J.M.,Barker, J.,Godemann, R.,Kraemer, J.,Hallett, D. (deposition date: 2010-04-29, release date: 2010-07-14, Last modification date: 2024-11-06)

Primary citation

Madden, J.,Dod, J.R.,Godemann, R.,Kraemer, J.,Smith, M.,Biniszkiewicz, M.,Hallett, D.J.,Barker, J.,Dyekjaer, J.D.,Hesterkamp, T.
Fragment-based discovery and optimization of BACE1 inhibitors.
Bioorg.Med.Chem.Lett., 20:5329-5333, 2010

PubMed Abstract: A novel series of 2-aminobenzimidazole inhibitors of BACE1 has been discovered using fragment-based drug discovery (FBDD) techniques. The rapid optimization of these inhibitors using structure-guided medicinal chemistry is discussed.

PubMed: 20656487
DOI: 10.1016/j.bmcl.2010.06.089

Experimental method

X-RAY DIFFRACTION (2 Å)