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==Structure of BACE1 complex with a HEA-type inhibitor== | |||
<StructureSection load='4try' size='340' side='right'caption='[[4try]], [[Resolution|resolution]] 2.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4try]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TRY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=36D:N-[(2R,3S)-3-AMINO-2-HYDROXY-4-(THIOPHEN-2-YL)BUTANOYL]-L-NORVALINE'>36D</scene>, <scene name='pdbligand=TIH:BETA(2-THIENYL)ALANINE'>TIH</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4try FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4try OCA], [https://pdbe.org/4try PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4try RCSB], [https://www.ebi.ac.uk/pdbsum/4try PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4try ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://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> | |||
==See Also== | |||
*[[Beta secretase 3D structures|Beta secretase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Akaji K]] | |||
[[Category: Akiyama T]] | |||
[[Category: Nakagawa A]] | |||
[[Category: Sanjho A]] | |||
[[Category: Teruya K]] | |||
[[Category: Yamashita E]] |
Latest revision as of 18:17, 8 November 2023
Structure of BACE1 complex with a HEA-type inhibitorStructure of BACE1 complex with a HEA-type inhibitor
Structural highlights
FunctionBACE1_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] See AlsoReferences
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