3ixj: Difference between revisions
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==Crystal structure of beta-secretase 1 in complex with selective beta-secretase 1 inhibitor== | ==Crystal structure of beta-secretase 1 in complex with selective beta-secretase 1 inhibitor== | ||
<StructureSection load='3ixj' size='340' side='right' caption='[[3ixj]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='3ixj' size='340' side='right' caption='[[3ixj]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
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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> | <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> | ||
<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> | <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> | ||
<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=3ixj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ixj OCA], [http://pdbe.org/3ixj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ixj RCSB], [http://www.ebi.ac.uk/pdbsum/3ixj PDBsum]</span></td></tr> | <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=3ixj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ixj OCA], [http://pdbe.org/3ixj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ixj RCSB], [http://www.ebi.ac.uk/pdbsum/3ixj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ixj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/3ixj_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/3ixj_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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[[Category: Lindberg, J]] | [[Category: Lindberg, J]] | ||
[[Category: Nystrom, S]] | [[Category: Nystrom, S]] | ||
[[Category: Alternative splicing]] | |||
[[Category: Aspartyl protease]] | [[Category: Aspartyl protease]] | ||
[[Category: Bace]] | [[Category: Bace]] | ||
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[[Category: Inhibitor]] | [[Category: Inhibitor]] | ||
[[Category: Membrane]] | [[Category: Membrane]] | ||
[[Category: Polymorphism]] | |||
[[Category: Protease]] | [[Category: Protease]] | ||
[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
[[Category: Zymogen]] | [[Category: Zymogen]] | ||
Revision as of 12:19, 19 December 2018
Crystal structure of beta-secretase 1 in complex with selective beta-secretase 1 inhibitorCrystal structure of beta-secretase 1 in complex with selective beta-secretase 1 inhibitor
Structural highlights
Function[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.[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 PubMedHighly potent BACE-1 protease inhibitors have been developed from an inhibitors containing a hydroxyethylene (HE) core displaying aryloxymethyl or benzyloxymethyl P1 side chain and a methoxy P1' side chain. The target molecules were synthesized in good overall yields from chiral carbohydrate starting materials. The inhibitors show high BACE-1 potency and good selectivity against cathepsin D, where the most potent inhibitor furnishes BACE-1 K(i) << 1 nM and displays >1000-fold selectivity over cathepsin D. Design and synthesis of potent and selective BACE-1 inhibitors.,Bjorklund C, Oscarson S, Benkestock K, Borkakoti N, Jansson K, Lindberg J, Vrang L, Hallberg A, Rosenquist A, Samuelsson B J Med Chem. 2010 Feb 25;53(4):1458-64. PMID:20128595[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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