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5owo
From Proteopedia
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==Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution== | ==Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution== | ||
| - | <StructureSection load='5owo' size='340' side='right' caption='[[5owo]], [[Resolution|resolution]] 1.79Å' scene=''> | + | <StructureSection load='5owo' size='340' side='right'caption='[[5owo]], [[Resolution|resolution]] 1.79Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5owo]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[5owo]] is a 4 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=5OWO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OWO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand= | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=5owo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5owo OCA], [https://pdbe.org/5owo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5owo RCSB], [https://www.ebi.ac.uk/pdbsum/5owo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5owo ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/DYHC1_HUMAN DYHC1_HUMAN] Autosomal dominant childhood-onset proximal spinal muscular atrophy without contractures;Autosomal dominant non-syndromic intellectual disability;Autosomal dominant Charcot-Marie-Tooth disease type 2O. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. |
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/DYHC1_HUMAN DYHC1_HUMAN] Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Plays a role in mitotic spindle assembly and metaphase plate congression (PubMed:27462074).<ref>PMID:27462074</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5owo" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5owo" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Dynein 3D structures|Dynein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Homo sapiens]] |
| - | [[Category: Carter | + | [[Category: Large Structures]] |
| - | [[Category: Elshenawy | + | [[Category: Carter AP]] |
| - | [[Category: Lau | + | [[Category: Elshenawy MM]] |
| - | [[Category: Morales-Rios | + | [[Category: Lau CK]] |
| - | [[Category: Motz | + | [[Category: Morales-Rios E]] |
| - | [[Category: Urnavicius | + | [[Category: Motz C]] |
| - | [[Category: Yildiz | + | [[Category: Urnavicius L]] |
| - | + | [[Category: Yildiz A]] | |
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Current revision
Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution
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