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 Jan 17;7:40674. doi: 10.1038/srep40674

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) A cartoon diagram depicts the final frame from a 40ns molecular dynamics simulation of a model of the coiled-coil interaction between EmMBD2/3 (cyan) and EmGATAD2A/B (blue). The amino acids residues conserved between the human and E. muelleri complexes (shown in sticks) are primarily located at the interface between the proteins. Expanded views (dashed boxes) show preservation of three critical ionic and hydrogen bond interactions, with the only difference between species involving a conservative aspartate to glutamate (E330) change (highlighted in magenta). (b) Alignment of the coiled-coil domains shows relatively low overall identity but with conservation of critical ionic (blue) and interface residues. (c) Analytical ultracentrifugation sedimentation velocity analyses indicates that the isolated EmMBD2/3 (black) and EmGATAD2A/B (blue) are largely monomeric while a mixture of the two (red) sediments as a combination of monomeric and heterodimeric species. (d) Isothermal titration calorimetry shows that the EmMBD2/3:EmGATAD2A/B and DmMBD2/3:DmGATAD2A/B complexes bind with relatively low affinity as compared to HsMBD2:HsGATAD2A; whereas cross-species (Em:Hs) complexes bind with intermediate affinities. (e) Circular dichroism measurements show that the EmGATAD2A/B (blue) an EmMBD2/3 (red) domains have relatively low helical content in isolation. (f) Alignment of DmMBD2/3 and DmGATAD2A/B with human orthologs shows a higher degree of conservation as compared to sponge.