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

. 2014 Jul 29;42(15):9656–9665. doi: 10.1093/nar/gku680

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

© The Author(s) 2014. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

PMC Copyright notice

Figure 5. — Disruption of the interaction between Pot1pC and the 3′ end of 15mer switches Pot1-DBD to the 12mer-binding mode. (A) In the Pot1pC+9mer complex, nucleotides G7 and T9 of 9mer (corresponding to G13 and T15 in 15mer) form an extended aromatic stack with Trp223 and Tyr224 of Pot1pC/Pot1DBD (PDB ID: 4HIK). Pot1pC is colored green, 9mer is colored violet and atoms are colored by element. (B) Y224A mutation disrupts binding of Pot1pC to 9mer by nearly 10-fold. (C) The same Y224A mutation in Pot1-DBD (blue) has no effect on affinity relative to wild-type Pot1-DBD (red). (D) However, Y224A mutation apparently switches to the 12mer-binding mode based on the supershift (red arrow) at high protein concentration. G13C substitution also creates a supershift indicative of the 12mer-binding mode.