2QK5

Structure of BACE1 bound to SCH626485

Summary for 2QK5

• Entry DOI: 10.2210/pdb2qk5/pdb
• Related: 2qkj 2qmd 2qmf 2qmg 2qp8
• Descriptor: Beta-secretase 1, N'-{(1S,2R)-1-(3,5-DIFLUOROBENZYL)-2-HYDROXY-3-[(3-METHOXYBENZYL)AMINO]PROPYL}-5-METHYL-N,N-DIPROPYLISOPHTHALAMIDE (3 entities in total)
• Functional Keywords: bace1, protease, alternative splicing, aspartyl protease, glycoprotein, hydrolase, membrane, transmembrane, zymogen
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein: P56817
• Total number of polymer chains: 2
• Total formula weight: 89042.50

Authors

Strickland, C.O.,Iserloh, U. (deposition date: 2007-07-10, release date: 2008-03-11, Last modification date: 2024-10-16)

Primary citation

Iserloh, U.,Wu, Y.,Cumming, J.N.,Pan, J.,Wang, L.Y.,Stamford, A.W.,Kennedy, M.E.,Kuvelkar, R.,Chen, X.,Parker, E.M.,Strickland, C.,Voigt, J.
Potent pyrrolidine- and piperidine-based BACE-1 inhibitors.
Bioorg.Med.Chem.Lett., 18:414-417, 2008

PubMed Abstract: Based on lead compound 1 identified from the patent literature, we developed novel patentable BACE-1 inhibitors by introducing a cyclic amine scaffold. Extensive SAR studies on both pyrrolidines and piperidines ultimately led to inhibitor 2f, one of the most potent inhibitors synthesized to date.

PubMed: 18023580
DOI: 10.1016/j.bmcl.2007.10.116

Experimental method

X-RAY DIFFRACTION (2.2 Å)