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. 2015 May 8;3(3):e00147. doi: 10.1002/prp2.147

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© 2015 The Authors. Pharmacology Research & Perspectives published by John Wiley & Sons Ltd, British Pharmacological Society and American Society for Pharmacology and Experimental Therapeutics.

This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Effects of PAPS/PAP-binding on the mobility (RMSF) of amino acids 208–273, including Loop 3 (aa 235–268) and a portion of the dimerization domain (aa 266–275). (A) Subunit A of simulations [1], [2], and [3]. (B) Subunit B of simulations [1], [2], and [3]. A relatively high level of stability was observed for residue 250 across simulations (trough indicated by black arrow). The key indicates the PAP/PAPS-binding state of each subunit. A secondary structure map of the highlighted region is available toward the bottom of the graph (L3 = Loop 3, green cylinders = α-helix).