4ivt
Crystal structure of BACE1 with its inhibitorCrystal structure of BACE1 with its inhibitor
FunctionFunction
[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]
About this StructureAbout this Structure
4ivt is a 1 chain structure. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Zou Y, Li L, Chen W, Chen T, Ma L, Wang X, Xiong B, Xu Y, Shen J. Virtual screening and structure-based discovery of indole acylguanidines as potent beta-secretase (BACE1) inhibitors. Molecules. 2013 May 16;18(5):5706-22. doi: 10.3390/molecules18055706. PMID:23681056 doi:http://dx.doi.org/10.3390/molecules18055706
- ↑ Lin X, Koelsch G, Wu S, Downs D, Dashti A, Tang J. Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1456-60. PMID:10677483
- ↑ Okada H, Zhang W, Peterhoff C, Hwang JC, Nixon RA, Ryu SH, Kim TW. Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing. FASEB J. 2010 Aug;24(8):2783-94. doi: 10.1096/fj.09-146357. Epub 2010 Mar 30. PMID:20354142 doi:10.1096/fj.09-146357