5owo
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5owo]] is a 4 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/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=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5owo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5owo OCA], [http://pdbe.org/5owo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5owo RCSB], [http://www.ebi.ac.uk/pdbsum/5owo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5owo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://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 == | ||
| + | [[http://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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 A resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine. | ||
| - | + | Cryo-EM shows how dynactin recruits two dyneins for faster movement.,Urnavicius L, Lau CK, Elshenawy MM, Morales-Rios E, Motz C, Yildiz A, Carter AP Nature. 2018 Feb 7;554(7691):202-206. doi: 10.1038/nature25462. PMID:29420470<ref>PMID:29420470</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5owo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Carter, A P]] | ||
| + | [[Category: Elshenawy, M M]] | ||
| + | [[Category: Lau, C K]] | ||
[[Category: Morales-Rios, E]] | [[Category: Morales-Rios, E]] | ||
| - | [[Category: Yildiz, A]] | ||
| - | [[Category: Lau, C.K]] | ||
[[Category: Motz, C]] | [[Category: Motz, C]] | ||
| - | [[Category: Carter, A.P]] | ||
| - | [[Category: Elshenawy, M.M]] | ||
[[Category: Urnavicius, L]] | [[Category: Urnavicius, L]] | ||
| + | [[Category: Yildiz, A]] | ||
| + | [[Category: Dimerization domain]] | ||
| + | [[Category: Dynein]] | ||
| + | [[Category: Heavy chain]] | ||
| + | [[Category: Motor protein]] | ||
Revision as of 05:35, 11 July 2018
Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution
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