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. Author manuscript; available in PMC: 2024 Jul 1.
Published in final edited form as: Cancer Lett. 2023 May 2;565:216207. doi: 10.1016/j.canlet.2023.216207

Figure 2.

Figure 2.

Structural features of the kinase domain of LIMK2. Kinase domain of LIMK2 showing the residues which form catalytic spine (C-spine) and regulatory spine (R-spine). We also show various catalytic subdomains of LIMK2, including αC loop, αG loop, αF-αG loop, glycine rich loop, catalytic loop, and partial activation segment. The catalytic loop of LIMK2 contains DLNSHN sequence, which matches neither tyrosine kinases nor Ser/Thr kinases. The R-spine is a hallmark of every active kinase, and consists of four residues, two from the C-lobe and two from the N-lobe. H449 residue is from the HRD motif in the catalytic loop. F391 is from the DFG motif in the activation segment. M380 is the conserved aliphatic residue from the αC-helix, and F470 is an aliphatic aminoacid from the β4-strand. The C-spine consists of a series of hydrophobic residues and is completed after ATP binds. The structure was created using AlphaFold2.