3bug

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{{Seed}}
 
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[[Image:3bug.png|left|200px]]
 
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==BACE-1 complexed with compound 3==
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The line below this paragraph, containing "STRUCTURE_3bug", creates the "Structure Box" on the page.
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<StructureSection load='3bug' size='340' side='right'caption='[[3bug]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3bug]] is a 1 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=3BUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BUG FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AEH:4-(2-AMINOETHYL)-2-ETHYLPHENOL'>AEH</scene></td></tr>
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{{STRUCTURE_3bug| PDB=3bug | SCENE= }}
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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=3bug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bug OCA], [https://pdbe.org/3bug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bug RCSB], [https://www.ebi.ac.uk/pdbsum/3bug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bug ProSAT]</span></td></tr>
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</table>
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== Function ==
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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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/3bug_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bug ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Fragment screening revealed that tyramine binds to the active site of the Alzheimer's disease drug target BACE-1. Hit expansion by selection of compounds from the Roche compound library identified tyramine derivatives with improved binding affinities as monitored by surface plasmon resonance. X-ray structures show that the amine of the tyramine fragment hydrogen-bonds to the catalytic water molecule. Structure-guided ligand design led to the synthesis of further low molecular weight compounds that are starting points for chemical leads.
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===BACE-1 complexed with compound 3===
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Tyramine fragment binding to BACE-1.,Kuglstatter A, Stahl M, Peters JU, Huber W, Stihle M, Schlatter D, Benz J, Ruf A, Roth D, Enderle T, Hennig M Bioorg Med Chem Lett. 2008 Feb 15;18(4):1304-7. Epub 2008 Jan 11. PMID:18226904<ref>PMID:18226904</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3bug" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18226904}}, adds the Publication Abstract to the page
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*[[Beta secretase 3D structures|Beta secretase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18226904 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18226904}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3BUG is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BUG OCA].
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==Reference==
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<ref group="xtra">PMID:18226904</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Memapsin 2]]
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[[Category: Large Structures]]
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[[Category: Hennig, M.]]
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[[Category: Hennig M]]
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[[Category: Kuglstatter, A.]]
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[[Category: Kuglstatter A]]
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[[Category: Alternative splicing]]
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[[Category: Alzheimer's disease]]
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[[Category: Aspartic protease]]
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[[Category: Aspartyl protease]]
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[[Category: Beta-secretase]]
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[[Category: Fragment screen]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase]]
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[[Category: Memapsin 2]]
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[[Category: Membrane]]
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[[Category: Transmembrane]]
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[[Category: Zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 06:27:24 2009''
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Current revision

BACE-1 complexed with compound 3

PDB ID 3bug

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