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Article

Two-state displacement by the kinesin-14 Ncd stalk.

Biophysical chemistry - 1 Mar 2011

Hallen Mark A, Liang Zhang-Yi, Endow Sharyn A

Abstract excerpt

The nonprocessive kinesin-14 Ncd motor binds to microtubules and hydrolyzes ATP, undergoing a single displacement before releasing the microtubule. A lever-like rotation of the coiled-coil stalk is thought to drive Ncd displacements or steps along microtubules. Crystal structures and cryoelectron microscopy reconstructions imply that stalk rotation is correlated with ADP release and microtubule binding by the...

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Identifiers

PMID: 21288629
DOI: 10.1016/j.bpc.2011.01.001
PMCID: PMC3080049

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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