5wtq
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human proteasome-assembling chaperone PAC4== | |
| + | <StructureSection load='5wtq' size='340' side='right' caption='[[5wtq]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5wtq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WTQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WTQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></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=5wtq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wtq OCA], [http://pdbe.org/5wtq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wtq RCSB], [http://www.ebi.ac.uk/pdbsum/5wtq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wtq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PSMG4_HUMAN PSMG4_HUMAN]] Chaperone protein which promotes assembly of the 20S proteasome. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 26S proteasome is a large protein complex, responsible for degradation of ubiquinated proteins in eukaryotic cells. Eukaryotic proteasome formation is a highly ordered process that is assisted by several assembly chaperones. The assembly of its catalytic 20S core particle depends on at least five proteasome-specific chaperones, i.e., proteasome-assembling chaperons 1-4 (PAC1-4) and proteasome maturation protein (POMP). The orthologues of yeast assembly chaperones have been structurally characterized, whereas most mammalian assembly chaperones are not. In the present study, we determined a crystal structure of human PAC4 at 1.90-A resolution. Our crystallographic data identify a hydrophobic surface that is surrounded by charged residues. The hydrophobic surface is complementary to that of its binding partner, PAC3. The surface also exhibits charge complementarity with the proteasomal alpha4-5 subunits. This will provide insights into human proteasome-assembling chaperones as potential anticancer drug targets. | ||
| - | + | Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation.,Kurimoto E, Satoh T, Ito Y, Ishihara E, Okamoto K, Yagi-Utsumi M, Tanaka K, Kato K Protein Sci. 2017 May;26(5):1080-1085. doi: 10.1002/pro.3153. Epub 2017 Mar 16. PMID:28263418<ref>PMID:28263418</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5wtq" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Ishihara, E]] | [[Category: Ishihara, E]] | ||
[[Category: Ito, Y]] | [[Category: Ito, Y]] | ||
| + | [[Category: Kato, K]] | ||
| + | [[Category: Kurimoto, E]] | ||
| + | [[Category: Satoh, T]] | ||
| + | [[Category: Tanaka, K]] | ||
| + | [[Category: Chaperone]] | ||
| + | [[Category: Proteasome assembly chaperone]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 07:16, 24 May 2017
Crystal structure of human proteasome-assembling chaperone PAC4
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