This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4gid

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Structure of beta-secretase complexed with inhibitor

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4gid"

@@ Line 1: / Line 1: @@
 ==Structure of beta-secretase complexed with inhibitor==
-<StructureSection load='4gid' size='340' side='right' caption='[[4gid]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='4gid' size='340' side='right'caption='[[4gid]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4gid]] is a 4 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=4GID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GID FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4gid]] is a 4 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=4GID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GID FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0GH:N-[(2S)-1-({(2S,3R)-3-HYDROXY-1-[(2-METHYLPROPYL)AMINO]-1-OXOBUTAN-2-YL}AMINO)-3-PHENYLPROPAN-2-YL]-5-[METHYL(METHYLSULFONYL)AMINO]-N-[(1R)-1-PHENYLETHYL]BENZENE-1,3-DICARBOXAMIDE'>0GH</scene>, <scene name='pdbligand=LPD:L-PROLINAMIDE'>LPD</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]] 2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fkn|1fkn]], [[2g94|2g94]], [[2vkm|2vkm]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0GH:N-[(2S)-1-({(2S,3R)-3-HYDROXY-1-[(2-METHYLPROPYL)AMINO]-1-OXOBUTAN-2-YL}AMINO)-3-PHENYLPROPAN-2-YL]-5-[METHYL(METHYLSULFONYL)AMINO]-N-[(1R)-1-PHENYLETHYL]BENZENE-1,3-DICARBOXAMIDE'>0GH</scene>, <scene name='pdbligand=LPD:L-PROLINAMIDE'>LPD</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=4gid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gid OCA], [https://pdbe.org/4gid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gid RCSB], [https://www.ebi.ac.uk/pdbsum/4gid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gid 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=4gid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gid OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gid RCSB], [http://www.ebi.ac.uk/pdbsum/4gid PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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 ==
-The structure-based design, synthesis, and X-ray structure of protein-ligand complexes of exceptionally potent and selective beta-secretase inhibitors are described. The inhibitors are designed specifically to interact with S(1)' active site residues to provide selectivity over memapsin 1 and cathepsin D. Inhibitor 5 has exhibited exceedingly potent inhibitory activity (K(i) = 17 pM) and high selectivity over BACE 2 (&gt;7000-fold) and cathepsin D (&gt;250000-fold). A protein-ligand crystal structure revealed important molecular insight into these selectivities. These interactions may serve as an important guide to design selectivity over the physiologically important aspartic acid proteases.
-Structure-Based Design of Highly Selective beta-Secretase Inhibitors: Synthesis, Biological Evaluation, and Protein-Ligand X-ray Crystal Structure.,Ghosh AK, Venkateswara Rao K, Yadav ND, Anderson DD, Gavande N, Huang X, Terzyan S, Tang J J Med Chem. 2012 Sep 6. PMID:22954357<ref>PMID:22954357</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
-*[[Beta secretase|Beta secretase]]
+*[[Beta secretase 3D structures|Beta secretase 3D structures]]
 == References ==
 <references/>
@@ Line 27: / Line 18: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Memapsin 2]]
+[[Category: Large Structures]]
-[[Category: Anderson, D]]
+[[Category: Anderson D]]
-[[Category: Gavande, N]]
+[[Category: Gavande N]]
-[[Category: Ghosh, A]]
+[[Category: Ghosh A]]
-[[Category: Huang, X]]
+[[Category: Huang X]]
-[[Category: Tang, J]]
+[[Category: Tang J]]
-[[Category: Terzyan, S]]
+[[Category: Terzyan S]]
-[[Category: Venkateswara, R K]]
+[[Category: Venkateswara RK]]
-[[Category: Yadav, N]]
+[[Category: Yadav N]]
-[[Category: A-beta]]
-[[Category: Alzheimer]]
-[[Category: App]]
-[[Category: Aspartic protease]]
-[[Category: Bace]]
-[[Category: Beta secretase]]
-[[Category: Drug design]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Memapsin]]
-[[Category: Protease]]

4gid

From Proteopedia

Current revision

Structure of beta-secretase complexed with inhibitor

Structural highlights

Function

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox