Rho-associated protein kinase

spinqualitylabelsall models Human ROCK1 kinase domain complex with thiazole inhibitor (PDB code 4yve) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Rho-associated protein kinase (ROCK) is a Rho GTPase effector. ROCK has been shown to regulate cadherin function and thus cell-cell adhesion. ROCKs phosphorylate a large number of actin-binding proteins to modulate their functions. ROCKs are kinases belonging to the AGC (PKA/ PKG/PKC) family of serine-threonine specific protein kinases. Disease Aberrant ROCK expression and activation contribute to cancer development. ROCK levels are elevated in testicular, bladder and esophageal cancers. Relevance ROCK inhibitors have potential to be developed for treatment of glaucoma and other ocular diseases. Structural highlights ROCK contains several domains including (in ROCK1) a kinase domain (residues 76-338); a coiled-coil region (residues 339-1103) which contains a Rho-binding domain (residues 934-1015) and a pleckstrin homology and cysteine-rich domain (residues 1103-1320) at the C-terminal. ROCK1 inhibitor binds in a pocket making interactions with a glycine-rich loop. 3D structures of Rho-associated protein kinase Rho-associated protein kinase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman