View source for Kinesin

<StructureSection load='' size='350' side='right' scene='41/410296/Cv/1' caption='KIF1A Motor Domain complex with ADP and Mg+2 ion (green), [[2zfi]]'>

== Function ==

[[Kinesin|Kinesins]] are eukaryotic motor proteins which move along microtubules<ref>PMID:19773780</ref>.  Kinesin (KIF) is a dimer consisting of 2 heavy chains and two light chains.  The heavy chain contains the N-terminal globular motor domain (MD) residues 1-375, responsible for the motor activity of kinesin, a central flexible neck linker (FNL) coiled-coil stalk which intertwines to form the dimer and a small globular C-terminal domain which interacts with other proteins like the kinesin light chain.  The light chain (KLC) forms the tail region. The KLC contains a cargo binding domain which is called TPR (Tetratricopeptide repeat).  The KIFs are named by their gene number. KIF are organized into 14 families named kinesin-1  to kinesin-14. KIF contains a forkhead-associated domain (FHA) which is involved in phosphopeptide recognition.<br />
*'''KIF1A''' transports organelles along axonal microtubules.<br />
*'''KIF1C''' and '''KIF2''' are plus-ended directed microtubule motors.<br />
*'''KIF2C''', '''KIF22''' and '''KIF3B''' are plus-ended directed microtubule motors in mitotic cells<br />
*'''KIF5C''' see [[Structural_Analysis_of_Conformational_Changes_in_Kinesin_and_GTP-state_Microtubules_Upon_Binding]].<br />
*'''KIF13B''' transports VEGFR2 from the Golgi to the endothelial cell surface.<br />
*'''KIF16B''' is plus-ended directed microtubule motor involved in endosome transport and receptor recycling.<br />
*'''KIFC1''' transports DNA molecules along cytoskeleton filaments.<br />
*'''Kar3''' is kinesin protein in yeast.<br />
*'''Eg5''' or '''KIF11''' is a kinesin (See [[Kinesin-5]]) which participates in mitosis.<br />
*'''NOD''' is a ''Drosophila'' chromosome-associated kinesin.

See also [[CAP-Gly domain]].

== Disease ==
Mutations in KIF5A are involved in hereditary spastic paraplegia<ref>PMID:18203753</ref>.  Mutation in KIF1B is the cause of Charcot-Marie-Tooth disease <ref>PMID:14559185</ref>.  Mutations in KIF22 cause spondyloepimetaphyseal dysplasia<ref>PMID:23665482</ref>.

== Structural highlights ==
<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>. 

<scene name='41/410296/Cv/14'>Mg coordination site</scene>. 
== 3D Structures of Kinesin ==
[[Kinesin 3D Structures]]

</StructureSection>

== References ==
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