3MSL

Fragment Based Discovery and Optimisation of BACE-1 Inhibitors

Summary for 3MSL

• Entry DOI: 10.2210/pdb3msl/pdb
• Related: 3MSJ 3MSK 3MSM
• Descriptor: Beta-secretase 1, IODIDE ION, (3S)-3-(2-amino-5-chloro-1H-benzimidazol-1-yl)-N-(cyclohexylmethyl)pentanamide, ... (4 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: 46051.66

Authors

Smith, M.,Madden, J.,Barker, J. (deposition date: 2010-04-29, release date: 2010-07-14, Last modification date: 2024-10-30)

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 (2.4 Å)