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Article

Removal of tightly bound ADP induces distinct structural changes of the two tryptophan-containing regions of the ncd motor domain.

Journal of biochemistry - 1 Jul 2005

Morii Hisayuki, Shimizu Takashi, Mizuno Naoko, Edamatsu Masaki, Ogawa Kazuo, Shimizu Youské, Toyoshima Yoko Y

Abstract excerpt

ncd is a molecular motor belonging to the kinesin superfamily. In solution, it is a homo-dimer of a 700 amino acid polypeptide. The C-terminus of each polypeptide forms a globular domain of about 40 kDa, the motor domain with ATPase activity. The ATPase site of the motor domain of kinesin family members, including ncd, binds ADP tightly, the release of which is facilitated by microtubules during the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 16046453
DOI: 10.1093/jb/mvi104

Provenance

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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