Formation of Salt Bridges Mediates Internal Dimerization of Myosin VI Medial Tail Domain

Hyeong Jun Kim, Jen Hsin, Yanxin Liu, Paul R Selvin, Klaus J Schulten

Research output: Contribution to journalArticle

Abstract

The unconventional motor protein, myosin VI, is known to dimerize upon cargo binding to its C-terminal end. It has been shown that one of its tail domains, called the medial tail domain, is a dimerization region. The domain contains an unusual pattern of alternating charged residues and a few hydrophobic residues. To reveal the unknown dimerization mechanism of the medial tail domain, we employed molecular dynamics and single-molecule experimental techniques. Both techniques suggest that the formation of electrostatic-based interhelical salt bridges between oppositely charged residues is a key dimerization factor. For the dimerization to occur, the two identical helices within the dimer do not bind in a symmetric fashion, but rather with an offset of about one helical repeat. Calculations of the dimer-dissociation energy find the contribution of hydrophobic residues to the dimerization process to be minor; they also find that the asymmetric homodimer state is energetically favorable over a state of separate helices.

Original languageEnglish (US)
Pages (from-to)1443-1449
Number of pages7
JournalStructure
Volume18
Issue number11
DOIs
StatePublished - Nov 10 2010

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Dimerization
Salts
Molecular Dynamics Simulation
Static Electricity
myosin VI
Proteins

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Formation of Salt Bridges Mediates Internal Dimerization of Myosin VI Medial Tail Domain. / Kim, Hyeong Jun; Hsin, Jen; Liu, Yanxin; Selvin, Paul R; Schulten, Klaus J.

In: Structure, Vol. 18, No. 11, 10.11.2010, p. 1443-1449.

Research output: Contribution to journalArticle

Kim, Hyeong Jun ; Hsin, Jen ; Liu, Yanxin ; Selvin, Paul R ; Schulten, Klaus J. / Formation of Salt Bridges Mediates Internal Dimerization of Myosin VI Medial Tail Domain. In: Structure. 2010 ; Vol. 18, No. 11. pp. 1443-1449.
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