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

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 ?-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.

SUBMITTER: Tu D

PROVIDER: S-EPMC3061879 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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

Tu Daqi D Li Yiqun Y Song Hyun Kyu HK Toms Angela V AV Gould Christopher J CJ Ficarro Scott B SB Marto Jarrod A JA Goode Bruce L BL Eck Michael J MJ

PloS one 20110321 3

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 53 ...[more]

PMID: 21445309

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