Variable surface loops and myosin activity: Accessories to a motor

C. T. Murphy, J. A. Spudich

Research output: Contribution to journalArticle

37 Scopus citations

Abstract

The catalytic head of myosin is a globular structure that has historically been divided into three segments of 25, 50, and 20 kDa. The solvent-exposed, proteolytically-sensitive surface loops of myosin that join these three segments are highly variable in their sequences. While surface loops have not traditionally been thought to affect enzymatic activities, these loops lie near the ATP and actin-binding sites and have been implicated in the modulation of myosin's kinetic activities. In this work we review the wealth of data regarding the loops that has accumulated over the years and discuss the roles of the loops in contributing to the different activities displayed by different myosin isoforms.

Original languageEnglish (US)
Pages (from-to)139-151
Number of pages13
JournalJournal of Muscle Research and Cell Motility
Volume21
Issue number2
DOIs
StatePublished - Aug 21 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Cell Biology

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