6f1y
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6f1y is ON HOLD Authors: Urnavicius, L., Lau, C.K., Elshenawy, M.M., Morales-Rios, E., Motz, C., Yildiz, A., Carter, A.P. Description: Dynein light...) |
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==Dynein light intermediate chain region of the dynein tail/dynactin/BICDR1 complex== |
| + | <SX load='6f1y' size='340' side='right' viewer='molstar' caption='[[6f1y]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6f1y]] 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=6F1Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6F1Y FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6f1t|6f1t]], [[6f1u|6f1u]], [[6f1v|6f1v]]</td></tr> | ||
| + | <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]), DYNC1LI2, DNCLI2, LIC2 ([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=6f1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f1y OCA], [http://pdbe.org/6f1y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f1y RCSB], [http://www.ebi.ac.uk/pdbsum/6f1y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f1y 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> [[http://www.uniprot.org/uniprot/DC1L2_HUMAN DC1L2_HUMAN]] Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. | ||
| + | <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> |
| - | [[Category: Lau, C | + | <div class="pdbe-citations 6f1y" style="background-color:#fffaf0;"></div> |
| + | |||
| + | ==See Also== | ||
| + | *[[Dynein 3D structures|Dynein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Carter, A P]] | ||
| + | [[Category: Elshenawy, M M]] | ||
| + | [[Category: Lau, C K]] | ||
| + | [[Category: Morales-Rios, E]] | ||
[[Category: Motz, C]] | [[Category: Motz, C]] | ||
| - | [[Category: Carter, A.P]] | ||
| - | [[Category: Elshenawy, M.M]] | ||
[[Category: Urnavicius, L]] | [[Category: Urnavicius, L]] | ||
| - | [[Category: Morales-Rios, E]] | ||
[[Category: Yildiz, A]] | [[Category: Yildiz, A]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Cryo-em]] | ||
| + | [[Category: Motor protein]] | ||
Current revision
Dynein light intermediate chain region of 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
