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. Author manuscript; available in PMC: 2018 Nov 1.
Published in final edited form as: Semin Cell Dev Biol. 2017 Jun 1;71:68–74. doi: 10.1016/j.semcdb.2017.05.024

Figure 1. Structure of α-actinin dimmers.

Figure 1

The active homodimer form of α-actinin consists of a pair of subunits in an anti-parallel arrangement. Three main functional domains exist in the monomer. At the N-terminus, two CH domains (CH1 and CH2) comprise an actin binding domain (ABD). A series of four spectrin repeats (SR1-4) form the long rod-shaped domain and is the main region of monomer association. At the C-terminus, a pair of EF domains comprise the calmodulinlike domain (CaM). A4D denotes 19 amino acid region of the N-terminus that is specific to the α- actinin-4 protein.