Figure 9.

Comparison of the catalytic domain spatial structures of the human protein kinase Aurora A (AURKA, STK6, PDB: 2J4Z) and the protein of unknown function STALK (S_T AURKA LIKE KINASE, UniProt: A7PY12) from V. vinifera. "a" (marked by blue) ATP-binding regions in Aurora A and STALK; "b" (marked by red) is active site; "c", "d" (marked by green) are the most spatially variable regions between the two proteins; phosphorylated Thr residues (287, 288) in the Aurora A are marked by brown. In bold are marked the only discrepancies between the corresponding functionally important residues in Aurora A versus STALK: Asn146↔Arg31, Lys141↔Arg26 in "a"; Thr288↔Thr172 in variable region "c"; Pro297↔Ala181 in the DFGWSxxxxxxxRxTxCGTxDYLPPE motif of the activating loop; Val377↔Ile263 in the D2_type destruction box - Rxx(L/I)xxVxxHPW

Karpov et al. BMC Genomics 2010 11(Suppl 1):S14   doi:10.1186/1471-2164-11-S1-S14