Crystal Structure of the Roco4 Kinase Domain bound to AppCp from D. discoideum

PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE

Roco kinase structures give insights into the mechanism of Parkinson disease-related leucine-rich-repeat kinase 2 mutations.

Roco4 Kinase Domain, UNP residues 1019-1292

Ras of complex proteins and C-terminal of roc 4

GAMGGSEFPKSRLPTLADNEIEYEKQIGKGGFGLVHKGRLVKDKSVVAIKSLILGDSEGETEMIEKFQEFQREVFIMSNL
NHPNIVKLYGLMHNPPRMVMEFVPCGDLYHRLLDKAHPIKWSVKLRLMLDIALGIEYMQNQNPPIVHRDLRSPNIFLQSL
DENAPVCAKVADFGLSQQSVHSVSGLLGNFQWMAPETIGAEEESYTEKADTYSFAMILYTILTGEGPFDEYSYGKIKFIN
MIREEGLRPTIPEDCPPRLRNVIELCWSGDPKKRPHFSYIVKELSEL

100 mM Bis- Tris pH, 200 mM Na/K Tartrate; 11% PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

The same Protein in the in-active conformation

The G1179S mutant Protein bound to AppCp in the active conformation

The L1178T mutant Protein bound to AppCp in the active conformation

The dame protein bound to the ROCK Inhibitor H1152

HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT

Protein Kinase, LRRK2, ROCO, Kinase, ATP-binding, Nucleotide-binding, Serine/threonine-protein kinase, TRANSFERASE, SIGNALING PROTEIN

PTLADNEIEYEKQIGKGGFGLVHKGRLVKDKSVVAIKSLILGDSEGETEMIEKFQEFQREVFIMSNLNHPNIVKLYGLMH
NPPRMVMEFVPCGDLYHRLLDKAHPIKWSVKLRLMLDIALGIEYMQNQNPPIVHRDLRSPNIFLQSLDENAPVCAKVADF
GLSQQSVHSVSGLLGNFQWMAPETIGAEEESYTEKADTYSFAMILYTILTGEGPFDEYSYGKIKFINMIREEGLRPTIPE
DCPPRLRNVIELCWSGDPKKRPHFSYIVKELSEL