5dqc: Difference between revisions
Jump to navigation
Jump to search
New page: '''Unreleased structure''' The entry 5dqc is ON HOLD Authors: Ghosh, A.K., Bhavanam, S.R., Yen, T.-C., Rao, K.V., Downs, D., Huang, X., Mescar, A.D., Tang, J. Description: Co-crystal o... |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==Co-crystal of BACE1 with compound 0211== | ||
<StructureSection load='5dqc' size='340' side='right'caption='[[5dqc]], [[Resolution|resolution]] 2.47Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dqc]] 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=5DQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DQC 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]] 2.4651Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5E7:N-[(2S,3R)-3-HYDROXY-4-({(2S,3S)-3-HYDROXY-1-[(2-METHYLPROPYL)AMINO]-1-OXOBUTAN-2-YL}AMINO)-1-PHENYLBUTAN-2-YL]-5-[METHYL(METHYLSULFONYL)AMINO]-N-[(1R)-1-PHENYLETHYL]BENZENE-1,3-DICARBOXAMIDE'>5E7</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=5dqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dqc OCA], [https://pdbe.org/5dqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dqc RCSB], [https://www.ebi.ac.uk/pdbsum/5dqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dqc 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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Design, synthesis and evaluation of very potent and selective beta-Secretase 2 (memapsin 1, BACE 2) inhibitors are described. The inhibitors were designed specifically to interact with the S2'-site of beta-secretase 2 to provide >170,000-fold selectivity over beta-secretase (BACE 1) and >15,000-fold selectivity over cathepsin D. BACE 2 is implicated in Type 2 diabetes. The studies serve as an important guide to selective BACE 2 inhibitors. | |||
Design of Potent and Highly Selective Inhibitors for Human beta-Secretase 2 (Memapsin 1), a Target for Type 2 Diabetes.,Ghosh AK, Reddy BS, Yen YC, Cardenas E, Rao KV, Downs D, Huang X, Tang J, Mesecar AD Chem Sci. 2016 May 1;7:3117-3122. Epub 2016 Feb 4. PMID:27347366<ref>PMID:27347366</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5dqc" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Huang | *[[Beta secretase 3D structures|Beta secretase 3D structures]] | ||
[[Category: Mescar | == References == | ||
[[Category: Rao | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Bhavanam SR]] | |||
[[Category: Cardenas EL]] | |||
[[Category: Downs D]] | |||
[[Category: Ghosh AK]] | |||
[[Category: Huang X]] | |||
[[Category: Mescar AD]] | |||
[[Category: Rao KV]] | |||
[[Category: Tang J]] | |||
[[Category: Yen T-C]] | |||
Latest revision as of 00:54, 29 June 2023
Co-crystal of BACE1 with compound 0211Co-crystal of BACE1 with compound 0211
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] Publication Abstract from PubMedDesign, synthesis and evaluation of very potent and selective beta-Secretase 2 (memapsin 1, BACE 2) inhibitors are described. The inhibitors were designed specifically to interact with the S2'-site of beta-secretase 2 to provide >170,000-fold selectivity over beta-secretase (BACE 1) and >15,000-fold selectivity over cathepsin D. BACE 2 is implicated in Type 2 diabetes. The studies serve as an important guide to selective BACE 2 inhibitors. Design of Potent and Highly Selective Inhibitors for Human beta-Secretase 2 (Memapsin 1), a Target for Type 2 Diabetes.,Ghosh AK, Reddy BS, Yen YC, Cardenas E, Rao KV, Downs D, Huang X, Tang J, Mesecar AD Chem Sci. 2016 May 1;7:3117-3122. Epub 2016 Feb 4. PMID:27347366[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||