3ddt: Difference between revisions

← Older edit

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

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='3ddt' size='340' side='right'caption='[[3ddt]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ddt]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DDT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3DDT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ddt]] is a 3 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=3DDT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DDT FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.9&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3ddt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ddt OCA], [http://pdbe.org/3ddt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ddt RCSB], [http://www.ebi.ac.uk/pdbsum/3ddt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ddt ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3ddt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ddt OCA], [https://pdbe.org/3ddt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ddt RCSB], [https://www.ebi.ac.uk/pdbsum/3ddt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ddt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TRI63_HUMAN TRI63_HUMAN]] E3 ubiquitin ligase. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.<ref>PMID:11927605</ref>
+[https://www.uniprot.org/uniprot/TRI63_HUMAN TRI63_HUMAN] E3 ubiquitin ligase. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.<ref>PMID:11927605</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 20: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ddt ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The B-box motif is the defining feature of the TRIM family of proteins, characterized by a RING finger-B-box-coiled coil tripartite fold. We have elucidated the crystal structure of B-box 2 (B2) from MuRF1, a TRIM protein that supports a wide variety of protein interactions in the sarcomere and regulates the trophic state of striated muscle tissue. MuRF1 B2 coordinates two zinc ions through a cross-brace alpha/beta-topology typical of members of the RING finger superfamily. However, it self-associates into dimers with high affinity. The dimerization pattern is mediated by the helical component of this fold and is unique among RING-like folds. This B2 reveals a long shallow groove that encircles the C-terminal metal binding site ZnII and appears as the defining protein-protein interaction feature of this domain. A cluster of conserved hydrophobic residues in this groove and, in particular, a highly conserved aromatic residue (Y133 in MuRF1 B2) is likely to be central to this role. We expect these findings to aid the future exploration of the cellular function and therapeutic potential of MuRF1.
-Structural analysis of B-Box 2 from MuRF1: identification of a novel self-association pattern in a RING-like fold.,Mrosek M, Meier S, Ucurum-Fotiadis Z, von Castelmur E, Hedbom E, Lustig A, Grzesiek S, Labeit D, Labeit S, Mayans O Biochemistry. 2008 Oct 7;47(40):10722-30. Epub 2008 Sep 17. PMID:18795805<ref>PMID:18795805</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3ddt" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 28: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Mayans, O]]
+[[Category: Mayans O]]
-[[Category: Mrosek, M]]
+[[Category: Mrosek M]]
-[[Category: Coiled coil]]
-[[Category: Cytoplasm]]
-[[Category: Ligase]]
-[[Category: Metal-binding]]
-[[Category: Muscle protein]]
-[[Category: Nucleus]]
-[[Category: Polymorphism]]
-[[Category: Ring-like fold]]
-[[Category: Ubl conjugation pathway]]
-[[Category: Zinc]]
-[[Category: Zinc-binding motif]]
-[[Category: Zinc-finger]]