Literature summary for 5.6.1.3 extracted from

Yonekura, H.; Nomura, A.; Ozawa, H.; Tatsu, Y.; Yumoto, N.; Uyeda, T.Q.
Mechanism of tail-mediated inhibition of kinesin activities studied using synthetic peptides (2006), Biochem. Biophys. Res. Commun., 343, 420-427.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli of human conventional kinesin in which the C-terminus is truncated at residue 560 and 6-His is fused at the C-terminus	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	synthetic peptides derived from the tail of kinesin inhibit the protein's ATPase and motor activities. A peptide that spans residues 904-933 exhibits the strongest inhibitory effect on steady-state motility and ATPase activity, reflecting diminished binding of the ADP-bound kinesin head to the microtubule. Tail-mediated inhibition of kinesin activity is mainly the product of allosteric inhibition induced by the intramolecular binding of kinesin tail domain to the motor domain	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Subunits

Subunits	Comment	Organism
More	inhibition of kinesin activity by its tail is mainly the product of allosteric inhibition induced by the intramolecular binding of kinesin tail domain to the motor domain	Homo sapiens

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Release 2023.1 (January 2023)