Floppy proteins and the hidden sequences they use to communicate

Authors

DOI:

https://doi.org/10.25250/thescbr.brk659

Keywords:

protein, cancer, interaction specificity

Abstract

Our cells are filled with proteins. These proteins usually have a specific structure which help them to make the specific interactions we need to live. But how do short, floppy regions of proteins make such tight and specific interactions despite lacking any structure?

Author Biographies

  • Theresa Hwang, Massachusetts Institute of Technology

    PhD Student

  • Amy Keating, Massachusetts Institute of Technology

    Professor

Original article reference

Hwang, T., Parker, S. S., Hill, S. M., Grant, R. A., Ilunga, M. W., Sivaraman, V., Mouneimne, G., & Keating, A. E. (2022). Native proline-rich motifs exploit sequence context to target actin-remodeling Ena/VASP protein ENAH. ELife, 11. https://doi.org/10.7554/eLife.70680

Downloads

  • URL

Published

2022-10-11

Issue

Vol. 8 No. 4 (2022)

Section

Health & Physiology

License

Copyright (c) 2022 Theresa Hwang, Amy Keating

Creative Commons License

This work is licensed under a Creative Commons Attribution-ShareAlike 4.0 International License.