6f1v
From Proteopedia
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==C terminal region of the dynein heavy chains in the dynein tail/dynactin/BICDR1 complex== | ==C terminal region of the dynein heavy chains in the dynein tail/dynactin/BICDR1 complex== | ||
| - | < | + | <SX load='6f1v' size='340' side='right' viewer='molstar' caption='[[6f1v]], [[Resolution|resolution]] 3.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6f1v]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F1V OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[6f1v]] is a 2 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=6F1V OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6F1V FirstGlance]. <br> |
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6f1t|6f1t]], [[6f1u|6f1u]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6f1t|6f1t]], [[6f1u|6f1u]]</td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6f1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f1v OCA], [http://pdbe.org/6f1v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f1v RCSB], [http://www.ebi.ac.uk/pdbsum/6f1v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f1v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Disease == | == Disease == | ||
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== Function == | == 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> | [[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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6f1v" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Carter, A P]] | [[Category: Carter, A P]] | ||
[[Category: Elshenawy, M M]] | [[Category: Elshenawy, M M]] | ||
Current revision
C terminal region of the dynein heavy chains in the dynein tail/dynactin/BICDR1 complex
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Categories: Human | Large Structures | Carter, A P | Elshenawy, M M | Lau, C K | Morales-Rios, E | Motz, C | Urnavicius, L | Yildiz, A | Complex | Cryo-em | Motor protein
