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3j1t

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Revision as of 18:18, 11 August 2016

High affinity dynein microtubule binding domain - tubulin complex

Structural highlights

3j1t is a 3 chain structure with sequence from Bos taurus and Lk3 transgenic mice. The August 2014 RCSB PDB Molecule of the Month feature on Dynein by David Goodsell is 10.2210/rcsb_pdb/mom_2014_8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3j1u
Gene:	Dync1h1, Dhc1, Dnch1, Dnchc1, Dyhc (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[DYHC1_MOUSE] Defects in Dync1h1 are the cause of the 'Legs at odd angles' (LOA) phenotype, an autosomal dominant trait where affected animals display unusual twisting of the body and clenching of the hindlimbs when suspended by the tail. Heterozygotes suffer age-related progressive loss of muscle tone and locomotor ability without major reduction in life-span while homozygotes show a more severe phenotype with an inability to move or feed, and die within 24 hours of birth. LOA mutants display defects in migration of facial motor neuron cell bodies and impaired retrograde transport in spinal cord motor neurons. Defects in Dync1h1 are the cause of the Cramping 1 (Cra1) phenotype, an autosomal dominant trait where affected animals display unusual twisting of the body and clenching of the hindlimbs when suspended by the tail. Heterozygotes suffer age-related progressive loss of muscle tone and locomotor ability without major reduction in life-span while homozygotes show a more severe phenotype with an inability to move or feed, and die within 24 hours of birth.

Function

[DYHC1_MOUSE] 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.

Publication Abstract from PubMed

Cytoplasmic dynein is a microtubule-based motor required for intracellular transport and cell division. Its movement involves coupling cycles of track binding and release with cycles of force-generating nucleotide hydrolysis. How this is accomplished given the ~25 nanometers separating dynein's track- and nucleotide-binding sites is not understood. Here, we present a subnanometer-resolution structure of dynein's microtubule-binding domain bound to microtubules by cryo-electron microscopy that was used to generate a pseudo-atomic model of the complex with molecular dynamics. We identified large rearrangements triggered by track binding and specific interactions, confirmed by mutagenesis and single-molecule motility assays, which tune dynein's affinity for microtubules. Our results provide a molecular model for how dynein's binding to microtubules is communicated to the rest of the motor.

Structural basis for microtubule binding and release by dynein.,Redwine WB, Hernandez-Lopez R, Zou S, Huang J, Reck-Peterson SL, Leschziner AE Science. 2012 Sep 21;337(6101):1532-6. PMID:22997337^[1]

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

References

↑ Redwine WB, Hernandez-Lopez R, Zou S, Huang J, Reck-Peterson SL, Leschziner AE. Structural basis for microtubule binding and release by dynein. Science. 2012 Sep 21;337(6101):1532-6. PMID:22997337 doi:http://dx.doi.org/10.1126/science.1224151

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3j1t"

@@ Line 1: / Line 1: @@
 ==High affinity dynein microtubule binding domain - tubulin complex==
 <StructureSection load='3j1t' size='340' side='right' caption='[[3j1t]], [[Resolution|resolution]] 9.70&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j1u|3j1u]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Dync1h1, Dhc1, Dnch1, Dnchc1, Dyhc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3j1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j1t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j1t RCSB], [http://www.ebi.ac.uk/pdbsum/3j1t PDBsum]</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=3j1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j1t OCA], [http://pdbe.org/3j1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j1t RCSB], [http://www.ebi.ac.uk/pdbsum/3j1t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j1t ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3j1t" style="background-color:#fffaf0;"></div>
 ==See Also==

3j1t

From Proteopedia

Revision as of 18:18, 11 August 2016

High affinity dynein microtubule binding domain - tubulin complex

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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