Kinesin

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== Structural highlights ==
== Structural highlights ==
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<scene name='41/410296/Cv/5'>Active site</scene>. Residue <scene name='41/410296/Cv/6'>Arg216 is the key residue in KIF for the chemical cycling of ATPase and for the mechanical cycling</scene>. Arg216 pivots to enable <scene name='41/410296/Cv/7'>Mg-ADP</scene> release or the phosphate release. <scene name='41/410296/Cv/8'>Arg216 forms a latch</scene> in the KIF 'closed-state' before the Mg-ADP release. Binding of β-tubulin to KIF releases the latch, enabling the KIF conformation change and detaching KIF from the microtubule and enabling the next movement cycle<ref>PMID:18806800</ref>. Water molecules shown as red spheres.
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<scene name='41/410296/Cv/10'>Active site</scene>. Water molecules shown as red spheres. Residue <scene name='41/410296/Cv/11'>Arg216 is the key residue in KIF for the chemical cycling of ATPase and for the mechanical cycling</scene>. Arg216 pivots to enable <scene name='41/410296/Cv/12'>Mg-ADP</scene> release or the phosphate release. <scene name='41/410296/Cv/13'>Arg216 forms a latch</scene> in the KIF 'closed-state' before the Mg-ADP release. Binding of β-tubulin to KIF releases the latch, enabling the KIF conformation change and detaching KIF from the microtubule and enabling the next movement cycle<ref>PMID:18806800</ref>.
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<scene name='41/410296/Cv/9'>Mg coordination site</scene>.
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<scene name='41/410296/Cv/14'>Mg coordination site</scene>.
</StructureSection>
</StructureSection>
== 3D Structures of Kinesin ==
== 3D Structures of Kinesin ==

Revision as of 10:51, 3 July 2019

KIF1A Motor Domain complex with ADP and Mg+2 ion (green), 2zfi

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3D Structures of Kinesin

Updated on 03-July-2019

References

  1. ↑ Hirokawa N, Noda Y, Tanaka Y, Niwa S. Kinesin superfamily motor proteins and intracellular transport. Nat Rev Mol Cell Biol. 2009 Oct;10(10):682-96. doi: 10.1038/nrm2774. PMID:19773780 doi:http://dx.doi.org/10.1038/nrm2774
  2. ↑ Ebbing B, Mann K, Starosta A, Jaud J, Schols L, Schule R, Woehlke G. Effect of spastic paraplegia mutations in KIF5A kinesin on transport activity. Hum Mol Genet. 2008 May 1;17(9):1245-52. doi: 10.1093/hmg/ddn014. Epub 2008 Jan, 18. PMID:18203753 doi:http://dx.doi.org/10.1093/hmg/ddn014
  3. ↑ Hirokawa N, Takemura R. Biochemical and molecular characterization of diseases linked to motor proteins. Trends Biochem Sci. 2003 Oct;28(10):558-65. PMID:14559185 doi:http://dx.doi.org/10.1016/j.tibs.2003.08.006
  4. ↑ Grosch M, Gruner B, Spranger S, Stutz AM, Rausch T, Korbel JO, Seelow D, Nurnberg P, Sticht H, Lausch E, Zabel B, Winterpacht A, Tagariello A. Identification of a Ninein (NIN) mutation in a family with spondyloepimetaphyseal dysplasia with joint laxity (leptodactylic type)-like phenotype. Matrix Biol. 2013 Oct-Nov;32(7-8):387-92. doi: 10.1016/j.matbio.2013.05.001. Epub, 2013 May 9. PMID:23665482 doi:http://dx.doi.org/10.1016/j.matbio.2013.05.001
  5. ↑ Nitta R, Okada Y, Hirokawa N. Structural model for strain-dependent microtubule activation of Mg-ADP release from kinesin. Nat Struct Mol Biol. 2008 Oct;15(10):1067-75. Epub 2008 Sep 21. PMID:18806800 doi:10.1038/nsmb.1487
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