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5a0q

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'''Unreleased structure'''
 
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The entry 5a0q is ON HOLD until sometime in the future
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==Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core==
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<SX load='5a0q' size='340' side='right' viewer='molstar' caption='[[5a0q]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5a0q]] is a 20 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=5A0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A0Q FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KNM:ADA-(AHX)3-(LEU)3-VINYL+SULFONE'>KNM</scene></td></tr>
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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=5a0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0q OCA], [https://pdbe.org/5a0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a0q RCSB], [https://www.ebi.ac.uk/pdbsum/5a0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a0q ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PSA6_HUMAN PSA6_HUMAN] The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The proteasome is a highly regulated protease complex fundamental for cell homeostasis and controlled cell cycle progression. It functions by removing a wide range of specifically tagged proteins, including key cellular regulators. Here we present the structure of the human 20S proteasome core bound to a substrate analogue inhibitor molecule, determined by electron cryo-microscopy (cryo-EM) and single-particle analysis at a resolution of around 3.5 A. Our map allows the building of protein coordinates as well as defining the location and conformation of the inhibitor at the different active sites. These results open new prospects to tackle the proteasome functional mechanisms. Moreover, they also further demonstrate that cryo-EM is emerging as a realistic approach for general structural studies of protein-ligand interactions.
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Authors: daFonseca, P.C.A., Morris, E.P.
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Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core.,da Fonseca PC, Morris EP Nat Commun. 2015 Jul 2;6:7573. doi: 10.1038/ncomms8573. PMID:26133119<ref>PMID:26133119</ref>
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Description: Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Morris, E.P]]
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<div class="pdbe-citations 5a0q" style="background-color:#fffaf0;"></div>
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[[Category: Dafonseca, P.C.A]]
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==See Also==
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*[[Proteasome 3D structures|Proteasome 3D structures]]
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Morris EP]]
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[[Category: DaFonseca PCA]]

Current revision

Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core

5a0q, resolution 3.50Å

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OCA

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