3unb: Difference between revisions

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-[[Image:3unb.png|left|200px]]
-<!--
+==Mouse constitutive 20S proteasome in complex with PR-957==
-The line below this paragraph, containing "STRUCTURE_3unb", creates the "Structure Box" on the page.
+<StructureSection load='3unb' size='340' side='right'caption='[[3unb]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3unb]] is a 40 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UNB FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=04C:1,2,4-TRIDEOXY-4-METHYL-2-{[N-(MORPHOLIN-4-YLACETYL)-L-ALANYL-O-METHYL-L-TYROSYL]AMINO}-1-PHENYL-D-XYLITOL'>04C</scene></td></tr>
-{{STRUCTURE_3unb|  PDB=3unb  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3unb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unb OCA], [https://pdbe.org/3unb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3unb RCSB], [https://www.ebi.ac.uk/pdbsum/3unb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3unb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PSB7_MOUSE PSB7_MOUSE] 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. This unit is responsible of the trypsin-like activity of the proteasome (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Constitutive proteasomes and immunoproteasomes shape the peptide repertoire presented by major histocompatibility complex class I (MHC-I) molecules by harboring different sets of catalytically active subunits. Here, we present the crystal structures of constitutive proteasomes and immunoproteasomes from mouse in the presence and absence of the epoxyketone inhibitor PR-957 (ONX 0914) at 2.9 A resolution. Based on our X-ray data, we propose a unique catalytic feature for the immunoproteasome subunit beta5i/LMP7. Comparison of ligand-free and ligand-bound proteasomes reveals conformational changes in the S1 pocket of beta5c/X but not beta5i, thereby explaining the selectivity of PR-957 for beta5i. Time-resolved structures of yeast proteasome:PR-957 complexes indicate that ligand docking to the active site occurs only via the reactive head group and the P1 side chain. Together, our results support structure-guided design of inhibitory lead structures selective for immunoproteasomes that are linked to cytokine production and diseases like cancer and autoimmune disorders.
-===Mouse constitutive 20S proteasome in complex with PR-957===
+Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity.,Huber EM, Basler M, Schwab R, Heinemeyer W, Kirk CJ, Groettrup M, Groll M Cell. 2012 Feb 17;148(4):727-38. PMID:22341445<ref>PMID:22341445</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3unb" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_22341445}}, adds the Publication Abstract to the page
+*[[Proteasome|Proteasome]]
-(as it appears on PubMed at http://www.pubmed.gov), where 22341445 is the PubMed ID number.
+*[[Proteasome 3D structures|Proteasome 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_22341445}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-[[3unb]] is a 56 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNB OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:022341445</ref><references group="xtra"/>
 [[Category: Mus musculus]]
-[[Category: Basler, M.]]
+[[Category: Basler M]]
-[[Category: Groettrup, M.]]
+[[Category: Groettrup M]]
-[[Category: Groll, M.]]
+[[Category: Groll M]]
-[[Category: Heinemeyer, W.]]
+[[Category: Heinemeyer W]]
-[[Category: Huber, E.]]
+[[Category: Huber E]]
-[[Category: Kirk, C.]]
+[[Category: Kirk C]]
-[[Category: Schwab, R.]]
+[[Category: Schwab R]]
-[[Category: 20s proteasome comprises 28 subunit]]
-[[Category: Covalent binding of pr-957 to all active site]]
-[[Category: Each subunit adopts the fold of an antiparallel beta-sheet flanked by helice]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Protease]]
-[[Category: Regulatory complex]]