1W50

Apo Structure of BACE (Beta Secretase)

Summary for 1W50

Entry DOI	10.2210/pdb1w50/pdb
Related	1FKN 1M4H 1PY1 1SGZ 1UJJ 1UJK 1W51
Descriptor	BETA-SECRETASE 1, IODIDE ION (3 entities in total)
Functional Keywords	alternative splicing, alzheimer's disease, aspartic protease, aspartyl protease, base, beta-secretase, glycoprotein, hydrolase, memapsin 2, transmembrane, zymogen
Biological source	HOMO SAPIENS (HUMAN)
Cellular location	Membrane; Single-pass type I membrane protein: P56817
Total number of polymer chains	1
Total formula weight	46330.06
Authors	Patel, S.,Vuillard, L.,Cleasby, A.,Murray, C.W.,Yon, J. (deposition date: 2004-08-04, release date: 2004-09-23, Last modification date: 2023-12-13)
Primary citation	Patel, S.,Vuillard, L.,Cleasby, A.,Murray, C.W.,Yon, J. Apo and Inhibitor Complex Structures of Bace (Beta-Secretase) J.Mol.Biol., 343:407-, 2004 Cited by PubMed Abstract: Human BACE, also known as beta-secretase, shows promise as a potential therapeutic target for Alzheimer's disease. We determined the apo structure of BACE to 1.75 A, and a structure of a hydroxyethylamine inhibitor complex derived by soaking. These show significant active-site movements compared to previously described BACE structures. Additionally, the structures reveal two pockets that could be targeted by structure-based drug design. PubMed: 15451669 DOI: 10.1016/J.JMB.2004.08.018 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.75 Å)

Structure validation