3hw1: Difference between revisions
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<StructureSection load='3hw1' size='340' side='right'caption='[[3hw1]], [[Resolution|resolution]] 2.48Å' scene=''> | <StructureSection load='3hw1' size='340' side='right'caption='[[3hw1]], [[Resolution|resolution]] 2.48Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3hw1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3hw1]] 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=3HW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HW1 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.48Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EV2:3-PYRROLIDIN-1-YLQUINOXALIN-2-AMINE'>EV2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hw1 OCA], [https://pdbe.org/3hw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hw1 RCSB], [https://www.ebi.ac.uk/pdbsum/3hw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hw1 ProSAT]</span></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=3hw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hw1 OCA], [https://pdbe.org/3hw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hw1 RCSB], [https://www.ebi.ac.uk/pdbsum/3hw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hw1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Barker J]] | |||
[[Category: Barker | [[Category: Ebneth A]] | ||
[[Category: Ebneth | [[Category: Godemann R]] | ||
[[Category: Godemann | [[Category: Kramer J]] | ||
[[Category: Kramer | [[Category: Madden J]] | ||
[[Category: Madden | [[Category: Smith MA]] | ||
[[Category: Smith | |||
Revision as of 18:54, 1 November 2023
Structure of Bace (beta secretase) in complex with ligand EV2Structure of Bace (beta secretase) in complex with ligand EV2
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] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNovel 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. 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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