3S2O

Fragment based discovery and optimisation of bace-1 inhibitors

Replaces:  3MSM

Summary for 3S2O

• Entry DOI: 10.2210/pdb3s2o/pdb
• Related: 3MSJ 3MSK 3MSL 3MSM
• Descriptor: Beta-secretase 1, (3S)-3-(2-amino-5-chloro-1H-benzimidazol-1-yl)-N-[(1R,3S,5R,7R)-tricyclo[3.3.1.1~3,7~]dec-2-yl]pentanamide, IODIDE ION, ... (4 entities in total)
• Functional Keywords: protease, alzheimer's disease, aspartic protease, aspartyl protease, base, beta-secretase, glycoprotein, memapsin 2, amyloid precursor protein secretases, aspartic endopeptidases, fragment-based drug design, fluorescence polarisation, transmembrane, 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: 46089.71

Authors

Madden, J.,Godemann, R.,Smith, M.A.,Hallett, D.,Barker, J.,Kraemer, J. (deposition date: 2011-05-17, release date: 2011-06-01, Last modification date: 2024-11-27)

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 (2.6 Å)