3shj

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==Proteasome in complex with hydroxyurea derivative HU10==
==Proteasome in complex with hydroxyurea derivative HU10==
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<StructureSection load='3shj' size='340' side='right' caption='[[3shj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='3shj' size='340' side='right'caption='[[3shj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3shj]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SHJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3shj]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SHJ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H10:1-HYDROXY-1-[(2R)-4-{3-[(3S,5S,7S)-TRICYCLO[3.3.1.1~3,7~]DEC-1-YLOXY]PHENYL}BUT-3-YN-2-YL]UREA'>H10</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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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]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ryp|1ryp]]</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=H10:1-HYDROXY-1-[(2R)-4-{3-[(3S,5S,7S)-TRICYCLO[3.3.1.1~3,7~]DEC-1-YLOXY]PHENYL}BUT-3-YN-2-YL]UREA'>H10</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </span></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=3shj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shj OCA], [https://pdbe.org/3shj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3shj RCSB], [https://www.ebi.ac.uk/pdbsum/3shj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3shj ProSAT]</span></td></tr>
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<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=3shj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3shj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3shj RCSB], [http://www.ebi.ac.uk/pdbsum/3shj PDBsum]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/PSB6_YEAST PSB6_YEAST] The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that 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. It has an ATP-dependent proteolytic activity.
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Inhibitors with a new mechanism of action are needed for 20S proteasome (CP) inhibition owing to the ineffectiveness of current market drugs against some types of solid tumors. A novel class of nonpeptidic CP inhibitors has been developed, which display reversible and noncovalent binding. The structure-based design of these highly active and site-specific inhibitors revealed unexplored binding subpockets.
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Hydroxyureas as Noncovalent Proteasome Inhibitors.,Gallastegui N, Beck P, Arciniega M, Huber R, Hillebrand S, Groll M Angew Chem Int Ed Engl. 2011 Nov 21. doi: 10.1002/anie.201106010. PMID:22105886<ref>PMID:22105886</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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==See Also==
==See Also==
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*[[Proteasome|Proteasome]]
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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__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Proteasome endopeptidase complex]]
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Arciniega, M]]
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[[Category: Arciniega M]]
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[[Category: Beck, P]]
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[[Category: Beck P]]
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[[Category: Gallastegui, N]]
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[[Category: Gallastegui N]]
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[[Category: Groll, M]]
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[[Category: Groll M]]
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[[Category: Hillebrand, S]]
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[[Category: Hillebrand S]]
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[[Category: Huber, R]]
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[[Category: Huber R]]
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[[Category: Cancer]]
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[[Category: Drug development]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Immunology]]
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[[Category: Protein degradation]]
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[[Category: Ubiquitin]]
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[[Category: Unfolded protein substrate]]
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Current revision

Proteasome in complex with hydroxyurea derivative HU10

PDB ID 3shj

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