AXIN Shapes Tankyrase ARChitecture

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AXIN Shapes Tankyrase ARChitecture Sebastian Guettler Structure Volume 24, Issue 10, Pages 1625-1627 (October 2016) DOI: 10.1016/j.str.2016.09.003 Copyright © 2016 Elsevier Ltd Terms and Conditions

Figure 1 AXIN-Induced Conformational Changes in Tankyrase (A and B) Schematics of Tankyrase (TNKS) and AXIN1 (HPS, His-Pro-Ser-rich region; ARCs, ankyrin repeat clusters; SAM, sterile alpha motif domain; PARP, catalytic domain; TBM, Tankyrase-binding motif, with TBM2 bearing an unusual insertion [underlined]; RGS, regulator of G protein signaling domain; DAX, Dishevelled and Axin domain). (C) Bivalent AXIN1 can simultaneously bind ARCs 1+2, 4+5, or 2+5. In the apo state, and presumably when ARCs 1+2 or 4+5 are engaged, the ARCs freely sample a wide conformational range (left). When AXIN1 links ARCs 2 and 5, the ARCs adopt a more compact state with ARC5 placed closely to ARC2 (right). Structure 2016 24, 1625-1627DOI: (10.1016/j.str.2016.09.003) Copyright © 2016 Elsevier Ltd Terms and Conditions