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. 2015 Mar 3;23(3):558–570. doi: 10.1016/j.str.2015.01.011

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© 2015 The Authors

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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N-ter Lobe of CaM Binds to P1aABD with Higher Affinity Than the C-ter Lobe

(A) Schematic illustrations of plectin and CaM. CH, calponin homology domain; PD, plakin domain; ROD, coiled-coil rod domain; CTD, C-terminal domain. Arrows indicate positions of the first N-ter residue of P1aABD and P1aABD_Δ22 constructs, respectively. Schematic illustration of the P1a fragment used in the assays is shown in boxed area.

(B–E) ITC assays showing preferential binding of CaM_NL to P1aABD. (B) P1aABD (40 μM) was titrated with CaM_NL (400 μM). (C) P1aABD (40 μM) was titrated with CaM_CL (400 μM). (D) P1aABD/CaM_CL complex (40/60 μM) was titrated with CaM_NL (400 μM). (E) P1aABD/CaM_NL complex (40/60 μM) was titrated with CaM_CL (400 μM). Data are expressed as mean values ± SD. ND, not determined.