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An ATP-gate controls tubulin binding by the tethered head of kinesin-1

Kinesin-1 is a 2-headed molecular motor that walks along microtubules, with each step gated by ATP binding. Existing models for the gating mechanism propose a role for the microtubule lattice. We show that unpolymerised tubulin binds to kinesin-1, causing tubulin-activated ADP release. With no added...

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Autori principali: Alonso, Maria C., Drummond, Douglas R., Kain, Susan, Hoeng, Julia, Amos, Linda, Cross, Robert A.
Natura: Artigo
Lingua:Inglês
Pubblicazione: 2007
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC2504013/
https://ncbi.nlm.nih.gov/pubmed/17412962
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1126/science.1136985
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