4lxm

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lxm RCSB], [http://www.ebi.ac.uk/pdbsum/4lxm PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4lxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lxm RCSB], [http://www.ebi.ac.uk/pdbsum/4lxm PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/BACE1_HUMAN 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.<ref>PMID:10677483</ref> <ref>PMID:20354142</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 18:30, 25 December 2014

Crystal Structure of Human Beta Secretase in Complex with compound 12a

4lxm, resolution 2.30Å

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