2qzl
From Proteopedia
Crystal Structure of human Beta Secretase complexed with IXS
Structural highlights
Function[BACE1_HUMAN] Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA series of beta-site amyloid precursor protein cleaving enzyme (BACE-1) inhibitors containing a psi(CH2NH) reduced amide bond were synthesized. Incorporation of this reduced amide isostere as a non-cleavable peptide surrogate afforded inhibitors possessing low nanomolar potencies in both an enzymatic and cell-based assay. BACE-1 inhibition by a series of psi[CH2NH] reduced amide isosteres.,Coburn CA, Stachel SJ, Jones KG, Steele TG, Rush DM, DiMuzio J, Pietrak BL, Lai MT, Huang Q, Lineberger J, Jin L, Munshi S, Katharine Holloway M, Espeseth A, Simon A, Hazuda D, Graham SL, Vacca JP Bioorg Med Chem Lett. 2006 Jul 15;16(14):3635-8. Epub 2006 May 11. PMID:16690314[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Categories: Homo sapiens | Memapsin 2 | Munshi, S | Aspartyl protease | Bace | Glycoprotein | Hydrolase | Membrane | Transmembrane | Zymogen
