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4lxk

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Current revision (10:38, 21 December 2022) (edit) (undo)
 
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==Crystal Structure of Human Beta Secretase in Complex with compound 11d==
==Crystal Structure of Human Beta Secretase in Complex with compound 11d==
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<StructureSection load='4lxk' size='340' side='right' caption='[[4lxk]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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<StructureSection load='4lxk' size='340' side='right'caption='[[4lxk]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4lxk]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LXK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4lxk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LXK FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1YT:(1R,3S,4S,5R)-3-(4-AMINO-3-FLUORO-5-{[(2R)-1,1,1-TRIFLUORO-3-METHOXYPROPAN-2-YL]OXY}BENZYL)-5-[(3-TERT-BUTYLBENZYL)AMINO]TETRAHYDRO-2H-THIOPYRAN-4-OL+1-OXIDE'>1YT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1YT:(1R,3S,4S,5R)-3-(4-AMINO-3-FLUORO-5-{[(2R)-1,1,1-TRIFLUORO-3-METHOXYPROPAN-2-YL]OXY}BENZYL)-5-[(3-TERT-BUTYLBENZYL)AMINO]TETRAHYDRO-2H-THIOPYRAN-4-OL+1-OXIDE'>1YT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4lxa|4lxa]], [[4lxm|4lxm]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxk OCA], [https://pdbe.org/4lxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lxk RCSB], [https://www.ebi.ac.uk/pdbsum/4lxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lxk ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BACE, BACE1, KIAA1149 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Memapsin_2 Memapsin 2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.46 3.4.23.46] </span></td></tr>
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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=4lxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lxk OCA], [http://pdbe.org/4lxk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lxk RCSB], [http://www.ebi.ac.uk/pdbsum/4lxk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lxk ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== 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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[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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4lxk" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4lxk" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Beta secretase 3D structures|Beta secretase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Memapsin 2]]
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[[Category: Large Structures]]
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[[Category: Bourgier, E]]
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[[Category: Bourgier E]]
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[[Category: Rondeau, J M]]
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[[Category: Rondeau JM]]
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[[Category: Aspartyl protease]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Membrane]]
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[[Category: Structure-based drug design]]
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Current revision

Crystal Structure of Human Beta Secretase in Complex with compound 11d

PDB ID 4lxk

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