Dynein arm substructure and the orientation of arm-microtubule attachments

Jock Avolio, Stephen Lebduska, Peter Satir

Research output: Contribution to journalArticlepeer-review

30 Scopus citations


In the presence of AMP-PCP (β,γ-methyleneadenosine 5′-triphosphate), a non-hydrolyzable analog of ATP, negative stain images of increased morphological detail indicate that the dynein arm, attached to ciliary doublet microtubules, is composed of subunits including a cape, an elongated body and a head. The arrangement of these subunits makes it possible to distinguish A from B subfiber binding sites on a single arm and to demonstrate that the head of an extended arm on subfiber A of one ciliary doublet is capable of binding to subfiber B of an adjacent doublet in a specific orientation, which supports a key step in a current model of the mechanochemical cycle by which the arm produces microtubule sliding in the ciliary axoneme.

Original languageEnglish (US)
Pages (from-to)389-401
Number of pages13
JournalJournal of Molecular Biology
Issue number3
StatePublished - Mar 5 1984

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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