5nw4: Difference between revisions
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<StructureSection load='5nw4' size='340' side='right' caption='[[5nw4]], [[Resolution|resolution]] 8.70Å' scene=''> | <StructureSection load='5nw4' size='340' side='right' caption='[[5nw4]], [[Resolution|resolution]] 8.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5nw4]] is a 39 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[5nw4]] is a 39 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NW4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NW4 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> | </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='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=5nw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nw4 OCA], [http://pdbe.org/5nw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nw4 RCSB], [http://www.ebi.ac.uk/pdbsum/5nw4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nw4 ProSAT]</span></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=5nw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nw4 OCA], [http://pdbe.org/5nw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nw4 RCSB], [http://www.ebi.ac.uk/pdbsum/5nw4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nw4 ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Carter, A P]] | [[Category: Carter, A P]] | ||
Revision as of 10:57, 6 October 2017
Human cytoplasmic dynein-1 bound to dynactin and an N-terminal construct of BICD2Human cytoplasmic dynein-1 bound to dynactin and an N-terminal construct of BICD2
Structural highlights
Publication Abstract from PubMedCytoplasmic 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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