Crystal structure of a coiled-coil domain from human ROCK I

Daqi Tu, Yiqun Li, Hyun Kyu Song, Angela V. Toms, Christopher J. Gould, Scott B. Ficarro, Jarrod A. Marto, Bruce L. Goode, Michael J. Eck

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26 Citations (Scopus)

Abstract

The small GTPase Rho and one of its targets, Rho-associated kinase (ROCK), participate in a variety of actin-based cellular processes including smooth muscle contraction, cell migration, and stress fiber formation. The ROCK protein consists of an N-terminal kinase domain, a central coiled-coil domain containing a Rho binding site, and a C-terminal pleckstrin homology domain. Here we present the crystal structure of a large section of the central coiled-coil domain of human ROCK I (amino acids 535-700). The structure forms a parallel α-helical coiled-coil dimer that is structurally similar to tropomyosin, an actin filament binding protein. There is an unusual discontinuity in the coiled-coil; three charged residues (E613, R617 and D620) are positioned at what is normally the hydrophobic core of coiled-coil packing. We speculate that this conserved irregularity could function as a hinge that allows ROCK to adopt its autoinhibited conformation.

Original languageEnglish
Article numbere18080
JournalPloS one
Volume6
Issue number3
DOIs
Publication statusPublished - 2011

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)
  • General

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    Tu, D., Li, Y., Song, H. K., Toms, A. V., Gould, C. J., Ficarro, S. B., Marto, J. A., Goode, B. L., & Eck, M. J. (2011). Crystal structure of a coiled-coil domain from human ROCK I. PloS one, 6(3), [e18080]. https://doi.org/10.1371/journal.pone.0018080