Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2017 May 12;8:15233. doi: 10.1038/ncomms15233

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2017, The Author(s)

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

PMC Copyright notice

(a) Percentage of cis-proline for several proline residues determined from peak intensities in 2D NMR correlation spectra of hyper-pSer5 CTD2′, where the dotted line denotes the average percentage of cis-proline in the unphosphorylated state (left). This is depicted schematically for various heptad sequences in CTD2′ (right). (b) Model for the effect of Ser5 phosphorylation on the structure of the CTD. In the unphosphorylated state, the CTD exists in an ensemble of conformational states that favour prolines in the trans conformation (top). Hyper-pSer5 incorporation causes the CTD heptad repeats bearing the sequence motifs highlighted in a to undergo dramatic structural rearrangement driven by pSer5-dependent proline isomerization.