3hvg: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:3hvg.png|left|200px]]
-{{STRUCTURE_3hvg|  PDB=3hvg  |  SCENE=  }}
+==Structure of bace (beta secretase) in Complex with EV0==
+<StructureSection load='3hvg' size='340' side='right'caption='[[3hvg]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3hvg]] 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=3HVG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HVG 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]] 2.26&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EV0:2-AMINO-6-PROPYLPYRIMIDIN-4(3H)-ONE'>EV0</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3hvg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hvg OCA], [https://pdbe.org/3hvg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hvg RCSB], [https://www.ebi.ac.uk/pdbsum/3hvg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hvg 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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hv/3hvg_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=3hvg ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Novel nonpeptidic inhibitors of beta-secretase (BACE1) have been discovered by employing a fragment-based biochemical screening approach. A diverse library of 20000 low-molecular weight compounds were screened and yielded 26 novel hits that were confirmed by biochemical and surface plasmon resonance secondary assays. We describe here fragment inhibitors cocrystallized with BACE1 in a flap open and flap closed conformation as determined by X-ray crystallography.
-===Structure of bace (beta secretase) in Complex with EV0===
+Fragment-Based Discovery of BACE1 Inhibitors Using Functional Assays.,Godemann R, Madden J, Kramer J, Smith M, Fritz U, Hesterkamp T, Barker J, Hoppner S, Hallett D, Cesura A, Ebneth A, Kemp J Biochemistry. 2009 Oct 23. PMID:19799414<ref>PMID:19799414</ref>
-{{ABSTRACT_PUBMED_19799414}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 3hvg" style="background-color:#fffaf0;"></div>
-[[3hvg]] is a 3 chain structure of [[Beta secretase]] with 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=3HVG OCA].
 ==See Also==
-*[[Beta secretase|Beta secretase]]
+*[[Beta secretase 3D structures|Beta secretase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:019799414</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Memapsin 2]]
+[[Category: Large Structures]]
-[[Category: Barker, J.]]
+[[Category: Barker J]]
-[[Category: Ebneth, A.]]
+[[Category: Ebneth A]]
-[[Category: Godemann, R.]]
+[[Category: Godemann R]]
-[[Category: Kramer, J.]]
+[[Category: Kramer J]]
-[[Category: Madden, J.]]
+[[Category: Madden J]]
-[[Category: Smith, M A.]]
+[[Category: Smith MA]]
-[[Category: Alzheimer's disease]]
-[[Category: Amyloid precursor protein secretase]]
-[[Category: Aspartic endopeptidase]]
-[[Category: Aspartic protease]]
-[[Category: Aspartyl protease]]
-[[Category: Base]]
-[[Category: Beta-secretase]]
-[[Category: Disulfide bond]]
-[[Category: Fluorescence polarisation]]
-[[Category: Fragment-based drug design]]
-[[Category: Glycoprotein]]
-[[Category: Hydrolase]]
-[[Category: Memapsin 2]]
-[[Category: Protease]]
-[[Category: Transmembrane]]
-[[Category: Zymogen]]