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

. 2018 Feb 2;9:476. doi: 10.1038/s41467-017-02811-7

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

© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 3 — Phosphorylation of CRMP2 at Y479 induces oligomerization changes in CRMP2 structure. a (Left panel) Surface representation of a tetramer of CRMP2 (residues 13–516) showing the dimerization interface. Visible carboxy-terminal (C’) extensions of each chain are shown as ribbons. Reader-visible Y499 are labeled and shown in cyan. a (Right panel) Tetramerization interface between the dimers is shown. The position of Y479 at the interface is also highlighted in blue. Zoom-in shows the details of this interface comprising the carboxy-terminal helix of chain A and residues 372–379 of the neighboring chain B. b Crystal structure of the phosphomimetic mutant CRMP2–2E. (Left panel) Position of E479 is highlighted. (Right panel) Position of SUMOylation site, K374, is highlighted. c Superposition of CRMP2 wild-type tetramer structure and CRMP2–2E phosphomimetic mutant dimer structure. Zoom-in showing key differences at the tetramerization interface: chain A (green) of CRMP2 (residues 13–516) has the Y479 (blue) at the carboxy-terminal helix which interacts with the loop (gray) of chain B (orange). CRMP2–2E mutant (red) has E479 in the position. The mutation introduces a charge in the hydrophobic cavity, causing the carboxy-terminal helix to unwind and the tetramer to break