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==Diethylaminosulfur Trifluoride-Mediated Intramolecular Cyclization of 2-hydroxy-benzylureas to Fused Bicyclic Aminooxazoline Compounds and Evaluation of Their Biochemical Activity Against Beta-Secretase-1 (BACE-1)==
==Diethylaminosulfur Trifluoride-Mediated Intramolecular Cyclization of 2-hydroxy-benzylureas to Fused Bicyclic Aminooxazoline Compounds and Evaluation of Their Biochemical Activity Against Beta-Secretase-1 (BACE-1)==
<StructureSection load='4l7j' size='340' side='right' caption='[[4l7j]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
<StructureSection load='4l7j' size='340' side='right'caption='[[4l7j]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4l7j]] is a 1 chain structure 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=4L7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L7J FirstGlance]. <br>
<table><tr><td colspan='2'>[[4l7j]] 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=4L7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L7J FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1W2:2-[(3AS,7AR)-2-AMINO-3A-(2,4-DIFLUOROPHENYL)-3A,6,7,7A-TETRAHYDRO[1,3]OXAZOLO[4,5-C]PYRIDIN-5(4H)-YL]PYRIDINE-3-CARBONITRILE'>1W2</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.651&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l7g|4l7g]], [[4l7h|4l7h]], [[4lc7|4lc7]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1W2:2-[(3AS,7AR)-2-AMINO-3A-(2,4-DIFLUOROPHENYL)-3A,6,7,7A-TETRAHYDRO[1,3]OXAZOLO[4,5-C]PYRIDIN-5(4H)-YL]PYRIDINE-3-CARBONITRILE'>1W2</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BACE1, BACE, KIAA1149 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4l7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l7j OCA], [https://pdbe.org/4l7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l7j RCSB], [https://www.ebi.ac.uk/pdbsum/4l7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l7j ProSAT]</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=4l7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l7j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l7j RCSB], [http://www.ebi.ac.uk/pdbsum/4l7j PDBsum]</span></td></tr>
</table>
</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>


==See Also==
==See Also==
*[[Beta secretase|Beta secretase]]
*[[Beta secretase 3D structures|Beta secretase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Memapsin 2]]
[[Category: Large Structures]]
[[Category: Do, M K.Geck]]
[[Category: Dutcher D]]
[[Category: Dutcher, D]]
[[Category: Geck Do MK]]
[[Category: Huestis, M P]]
[[Category: Huestis MP]]
[[Category: Hunt, K W]]
[[Category: Hunt KW]]
[[Category: Liu, W]]
[[Category: Liu W]]
[[Category: Purkey, H E]]
[[Category: Purkey HE]]
[[Category: Siu, M]]
[[Category: Siu M]]
[[Category: Smith, D]]
[[Category: Smith D]]
[[Category: Vigers, G]]
[[Category: Vigers G]]
[[Category: Volgraf, M]]
[[Category: Volgraf M]]
[[Category: Wang, W]]
[[Category: Wang W]]
[[Category: Wu, P]]
[[Category: Wu P]]
[[Category: Yu, C]]
[[Category: Yu C]]
[[Category: Aspartic protease]]
[[Category: Hydrolase-hydrolase inhibitor complex]]

Latest revision as of 19:14, 20 September 2023

Diethylaminosulfur Trifluoride-Mediated Intramolecular Cyclization of 2-hydroxy-benzylureas to Fused Bicyclic Aminooxazoline Compounds and Evaluation of Their Biochemical Activity Against Beta-Secretase-1 (BACE-1)Diethylaminosulfur Trifluoride-Mediated Intramolecular Cyclization of 2-hydroxy-benzylureas to Fused Bicyclic Aminooxazoline Compounds and Evaluation of Their Biochemical Activity Against Beta-Secretase-1 (BACE-1)

Structural highlights

4l7j is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.651Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

See Also

References

  1. ↑ Lin X, Koelsch G, Wu S, Downs D, Dashti A, Tang J. Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein. Proc Natl Acad Sci U S A. 2000 Feb 15;97(4):1456-60. PMID:10677483
  2. ↑ Okada H, Zhang W, Peterhoff C, Hwang JC, Nixon RA, Ryu SH, Kim TW. Proteomic identification of sorting nexin 6 as a negative regulator of BACE1-mediated APP processing. FASEB J. 2010 Aug;24(8):2783-94. doi: 10.1096/fj.09-146357. Epub 2010 Mar 30. PMID:20354142 doi:10.1096/fj.09-146357

4l7j, resolution 1.65Å

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