3hgz

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{{Seed}}
 
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[[Image:3hgz.png|left|200px]]
 
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==Crystal structure of human insulin-degrading enzyme in complex with amylin==
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The line below this paragraph, containing "STRUCTURE_3hgz", creates the "Structure Box" on the page.
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<StructureSection load='3hgz' size='340' side='right'caption='[[3hgz]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3hgz]] 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=3HGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HGZ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.91&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3hgz| PDB=3hgz | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hgz OCA], [https://pdbe.org/3hgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hgz RCSB], [https://www.ebi.ac.uk/pdbsum/3hgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hgz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IAPP_HUMAN IAPP_HUMAN] Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hg/3hgz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hgz ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Insulin-degrading enzyme (IDE) is involved in the clearance of many bioactive peptide substrates, including insulin and amyloid-beta, peptides vital to the development of diabetes and Alzheimer's disease, respectively. IDE can also rapidly degrade hormones that are held together by intramolecular disulfide bond(s) without their reduction. Furthermore, IDE exhibits a remarkable ability to preferentially degrade structurally similar peptides such as the selective degradation of insulin-like growth factor (IGF)-II and transforming growth factor-alpha (TGF-alpha) over IGF-I and epidermal growth factor, respectively. Here, we used high-accuracy mass spectrometry to identify the cleavage sites of human IGF-II, TGF-alpha, amylin, reduced amylin, and amyloid-beta by human IDE. We also determined the structures of human IDE-IGF-II and IDE-TGF-alpha at 2.3 A and IDE-amylin at 2.9 A. We found that IDE cleaves its substrates at multiple sites in a biased stochastic manner. Furthermore, the presence of a disulfide bond in amylin allows IDE to cut at an additional site in the middle of the peptide (amino acids 18-19). Our amylin-bound IDE structure offers insight into how the structural constraint from a disulfide bond in amylin can alter IDE cleavage sites. Together with NMR structures of amylin and the IGF and epidermal growth factor families, our work also reveals the structural basis of how the high dipole moment of substrates complements the charge distribution of the IDE catalytic chamber for the substrate selectivity. In addition, we show how the ability of substrates to properly anchor their N-terminus to the exosite of IDE and undergo a conformational switch upon binding to the catalytic chamber of IDE can also contribute to the selective degradation of structurally related growth factors.
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===Crystal structure of human insulin-degrading enzyme in complex with amylin===
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Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme.,Guo Q, Manolopoulou M, Bian Y, Schilling AB, Tang WJ J Mol Biol. 2010 Jan 15;395(2):430-43. Epub 2009 Nov 5. PMID:19896952<ref>PMID:19896952</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3hgz" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19896952}}, adds the Publication Abstract to the page
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*[[Insulin-degrading enzyme 3D structures|Insulin-degrading enzyme 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19896952 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19896952}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3HGZ is a 4 chains structure with sequences 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=3HGZ OCA].
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==Reference==
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<ref group="xtra">PMID:19896952</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Insulysin]]
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[[Category: Large Structures]]
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[[Category: Bian, Y.]]
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[[Category: Bian Y]]
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[[Category: Guo, Q.]]
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[[Category: Guo Q]]
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[[Category: Tang, W J.]]
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[[Category: Tang WJ]]
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[[Category: Amidation]]
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[[Category: Amylin]]
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[[Category: Amyloid]]
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[[Category: Cleavage on pair of basic residue]]
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[[Category: Cystein free]]
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[[Category: Cytoplasm]]
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[[Category: Disulfide bond]]
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[[Category: Hormone]]
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[[Category: Hydrolase]]
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[[Category: Ide]]
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[[Category: Insulin degrading enzyme]]
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[[Category: Metal-binding]]
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[[Category: Metalloprotease]]
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[[Category: Polymorphism]]
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[[Category: Protease]]
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[[Category: Secreted]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 28 14:35:32 2010''
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Current revision

Crystal structure of human insulin-degrading enzyme in complex with amylin

PDB ID 3hgz

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