The Protein Tango

By Bob Grant The Protein Tango Researchers unravel the complexities of coupled protein binding and folding and lead others towards new drug targets. pKID (orange) bound to KIX (blue) Image by Adrian Turjanski Proteins don’t typically behave tractably. The molecular interaction between two proteins is often a lot more complicated than one fully formed protein fitting into anot

Written byBob Grant
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Proteins don’t typically behave tractably. The molecular interaction between two proteins is often a lot more complicated than one fully formed protein fitting into another, lock-and-key style. Especially when considering the lightning-fast connections being formed, broken, and re-formed when signaling proteins interact. Some critical signaling proteins exist in highly disordered, or unfolded, forms and only fold into their final conformations when they encounter and engage their molecular dance partners.

But until Scripps Research Institute structural biologist Peter Wright and colleagues described the intricate and fast-paced dance between one of these “intrinsically disordered proteins” and its target, researchers were left to guess about the kinetics and structural changes involved in these pairings. Wright and his coauthors characterized the complex and fluid interaction between a disordered protein segment, the phosphorylated kinase–inducible activation domain (pKID) of the cAMP response element binding (CREB) transcription factor, and its binding partner, the KIX domain of the ...

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Meet the Author

  • From 2017 to 2022, Bob Grant was Editor in Chief of The Scientist, where he started in 2007 as a Staff Writer. Before joining the team, he worked as a reporter at Audubon and earned a master’s degree in science journalism from New York University. In his previous life, he pursued a career in science, getting a bachelor’s degree in wildlife biology from Montana State University and a master’s degree in marine biology from the College of Charleston in South Carolina. Bob edited Reading Frames and other sections of the magazine.

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