Crystal Structure of Human BACE2 in Complex with a Hydroxyethylamine Transition-state Inhibitor

BACE2 is a membrane-bound aspartic protease of the A1 family with a high level of sequence homology to BACE1. While BACE1 is involved in the generation of amyloid plaques in Alzheimer's disease by cleaving Aβ-peptides from the amyloid precursor protein, the physiological function of BACE2 is no...

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Veröffentlicht in:	Journal of molecular biology 2006-01, Vol.355 (2), p.249-261
Hauptverfasser:	Ostermann, Nils, Eder, Jörg, Eidhoff, Ulf, Zink, Florence, Hassiepen, Ulrich, Worpenberg, Susanne, Maibaum, Jürgen, Simic, Oliver, Hommel, Ulrich, Gerhartz, Bernd
Format:	Artikel
Sprache:	eng
Schlagworte:	activation Amino Acid Sequence Amyloid Precursor Protein Secretases Aspartic Acid Endopeptidases - antagonists & inhibitors Aspartic Acid Endopeptidases - chemistry Aspartic Acid Endopeptidases - genetics aspartic protease BACE2 Binding Sites crystal structure Crystallization Drug Design Enzyme Inhibitors - chemistry Enzyme Stability Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Ethanolamines - chemistry Humans Inclusion Bodies - enzymology Molecular Sequence Data Mutation Protein Structure, Secondary refolding Structure-Activity Relationship
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