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Fig. 4 Conformational dynamics of the activation loop of PKA-CWT and PKA-CL205R upon binding substrate. Conformational dynamics of the activation loop.

Published byChristoph Althaus Modified over 5 years ago

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Presentation on theme: "Fig. 4 Conformational dynamics of the activation loop of PKA-CWT and PKA-CL205R upon binding substrate. Conformational dynamics of the activation loop."— Presentation transcript:

1 Fig. 4 Conformational dynamics of the activation loop of PKA-CWT and PKA-CL205R upon binding substrate. Conformational dynamics of the activation loop of PKA-CWT and PKA-CL205R upon binding substrate. (A) Distinct opening-closing motions of the Gly-rich loop highlighting the hindered conformation that occludes the entering of ATP in PKA-CL205R. (B) Probability density describing the conformation of the activation loop in response to different substrates and pseudo-substrates. (C) [1H, 15N]-TROSY-HSQC spectra showing the backbone amide chemical shift changes of the W196 indole amide (located on the activation loop) in response to binding PKI or VPS36. (D) X-ray structure of PKA-CWT (gray) (PDB ID: 1ATP) with the overlay PKA-CL205R in complex with PKI (light blue) (PDB ID: 4WB6) describing the architecture of the peptide binding site and activation loop flip. (E) X-ray structure of PKA-CWT (gray) (PDB ID: 1ATP) with the overlay PKA-CL205R in complex with VPS36 (light blue) (MD simulations) describing the architecture of the peptide binding site and activation loop flip. Caitlin Walker et al. Sci Adv 2019;5:eaaw9298 Copyright © 2019 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).

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