1iru: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the mammalian 20S proteasome at 2.75 A resolution==
-<StructureSection load='1iru' size='340' side='right' caption='[[1iru]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
+<StructureSection load='1iru' size='340' side='right'caption='[[1iru]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1iru]] is a 28 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IRU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1iru]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IRU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IRU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</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=1iru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iru OCA], [http://pdbe.org/1iru PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iru RCSB], [http://www.ebi.ac.uk/pdbsum/1iru PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iru ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iru OCA], [https://pdbe.org/1iru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iru RCSB], [https://www.ebi.ac.uk/pdbsum/1iru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iru ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PSB3_BOVIN PSB3_BOVIN]] 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.
+[https://www.uniprot.org/uniprot/PSA6_BOVIN PSA6_BOVIN] Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).[UniProtKB:P60900]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ir/1iru_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ir/1iru_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Proteasome|Proteasome]]
+*[[Proteasome 3D structures|Proteasome 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bovin]]
+[[Category: Bos taurus]]
-[[Category: Mizushima, T]]
+[[Category: Large Structures]]
-[[Category: Morimoto, Y]]
+[[Category: Mizushima T]]
-[[Category: Tanaka, K]]
+[[Category: Morimoto Y]]
-[[Category: Tomisugi, Y]]
+[[Category: Tanaka K]]
-[[Category: Tsukihara, T]]
+[[Category: Tomisugi Y]]
-[[Category: Unno, M]]
+[[Category: Tsukihara T]]
-[[Category: Yasuoka, N]]
+[[Category: Unno M]]
-[[Category: 20s proteasome]]
+[[Category: Yasuoka N]]
-[[Category: Cell cycle]]
-[[Category: Hydrolase]]
-[[Category: Immune response]]
-[[Category: Proteolysis]]
-[[Category: Ubiquitin]]