3O0Z

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

Summary for 3O0Z

• Entry DOI: 10.2210/pdb3o0z/pdb
• Descriptor: Rho-associated protein kinase 1 (2 entities in total)
• Functional Keywords: coiled-coil, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q13464
• Total number of polymer chains: 4
• Total formula weight: 79574.68

Authors

Tu, D.,Eck, M.J. (deposition date: 2010-07-20, release date: 2011-03-23, Last modification date: 2024-10-16)

Primary citation

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.
Crystal Structure of a Coiled-Coil Domain from Human ROCK I.
Plos One, 6:e18080-e18080, 2011

PubMed 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.

PubMed: 21445309
DOI: 10.1371/journal.pone.0018080

Experimental method

X-RAY DIFFRACTION (2.33 Å)