View source for 5nvu


==Full length human cytoplasmic dynein-1 in the phi-particle conformation==
<SX load='5nvu' size='340' side='right' viewer='molstar' caption='[[5nvu]], [[Resolution|resolution]] 15.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nvu]] is a 13 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=5NVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NVU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 15&#8491;</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=5nvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nvu OCA], [https://pdbe.org/5nvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nvu RCSB], [https://www.ebi.ac.uk/pdbsum/5nvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nvu ProSAT]</span></td></tr>
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== Publication Abstract from PubMed ==
Cytoplasmic dynein-1 binds dynactin and cargo adaptor proteins to form a transport machine capable of long-distance processive movement along microtubules. However, it is unclear why dynein-1 moves poorly on its own or how it is activated by dynactin. Here, we present a cryoelectron microscopy structure of the complete 1.4-megadalton human dynein-1 complex in an inhibited state known as the phi-particle. We reveal the 3D structure of the cargo binding dynein tail and show how self-dimerization of the motor domains locks them in a conformation with low microtubule affinity. Disrupting motor dimerization with structure-based mutagenesis drives dynein-1 into an open form with higher affinity for both microtubules and dynactin. We find the open form is also inhibited for movement and that dynactin relieves this by reorienting the motor domains to interact correctly with microtubules. Our model explains how dynactin binding to the dynein-1 tail directly stimulates its motor activity.

Cryo-EM Reveals How Human Cytoplasmic Dynein Is Auto-inhibited and Activated.,Zhang K, Foster HE, Rondelet A, Lacey SE, Bahi-Buisson N, Bird AW, Carter AP Cell. 2017 Jun 15;169(7):1303-1314.e18. doi: 10.1016/j.cell.2017.05.025. Epub, 2017 Jun 8. PMID:28602352<ref>PMID:28602352</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Dynein 3D structures|Dynein 3D structures]]
== References ==
<references/>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Carter AP]]
[[Category: Foster HE]]
[[Category: Zhang K]]