6f1v

From Proteopedia

(Difference between revisions)

Current revision

C terminal region of the dynein heavy chains in the dynein tail/dynactin/BICDR1 complex

6f1v, resolution 3.40Å

Structural highlights

6f1v is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	6f1t, 6f1u
Gene:	DYNC1H1, DHC1, DNCH1, DNCL, DNECL, DYHC, KIAA0325 (HUMAN)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[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

[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).^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chu X, Chen X, Wan Q, Zheng Z, Du Q. Nuclear Mitotic Apparatus (NuMA) Interacts with and Regulates Astrin at the Mitotic Spindle. J Biol Chem. 2016 Sep 16;291(38):20055-67. doi: 10.1074/jbc.M116.724831. Epub, 2016 Jul 26. PMID:27462074 doi:http://dx.doi.org/10.1074/jbc.M116.724831
↑ Urnavicius L, Lau CK, Elshenawy MM, Morales-Rios E, Motz C, Yildiz A, Carter AP. Cryo-EM shows how dynactin recruits two dyneins for faster movement. Nature. 2018 Feb 7;554(7691):202-206. doi: 10.1038/nature25462. PMID:29420470 doi:http://dx.doi.org/10.1038/nature25462

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6f1v"

@@ Line 1: / Line 1: @@
 ==C terminal region of the dynein heavy chains in the dynein tail/dynactin/BICDR1 complex==
-<StructureSection load='6f1v' size='340' side='right'caption='[[6f1v]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
+<SX load='6f1v' size='340' side='right' viewer='molstar' caption='[[6f1v]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
 == Structural highlights ==
-<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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F1V FirstGlance]. <br>
+<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>
 <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://oca.weizmann.ac.il/oca-docs/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>
+<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>
 == Disease ==
@@ Line 24: / Line 24: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Human]]
 [[Category: Large Structures]]

6f1v

From Proteopedia

Current revision

C terminal region of the dynein heavy chains in the dynein tail/dynactin/BICDR1 complex

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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