Article
New insight on the S100A1–STIP1 complex highlights the important relationship between allostery and entropy in protein function
Biochemical Journal
(2017)
Abstract
Calcium signaling serves as a nexus of many vital cellular processes. Of particular importance is the role the calcium signaling plays in the prevention of protein misfolding, and the S100 family of calcium-binding proteins is a key player in this pathway. While the S100 proteins carry out a range of roles, the interaction of S100A1 and the stress-inducible phosphoprotein 1 (STIP1) has been shown to be particularly important. A recent study by Maciejewski et al. in Biochemical Journal (Biochemical Journal (2017) 474, 1853–1866) revealed new insights into the nature of the S100A1–STIP1 interaction. Not only did the present paper indicate the stoichiometry of binding for this interaction (three S100A1 dimers : one STIP1), it also demonstrated that the binding interaction is highly co-operative and that each S100A1–STIP1-binding interaction is entropically driven. The findings presented raise important new questions regarding the relationship between entropy and allostery in protein function. Recently, the dynamical underpinnings of allostery in protein function have become a topic of increased interest. A broad range of investigations have demonstrated that allostery can be mediated by entropic processes such as changes in the flexibility of the protein backbone and in the range of motions explored by side chains. The S100A1–STIP1 complex as described by Maciejewski et al. suggests a new system in which an allosteric-binding interaction driven by entropic processes may be systematically dissected in the future.
Disciplines
Publication Date
September 1, 2017
DOI
10.1042/BCJ20170275
Publisher Statement
© 2017 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.
Citation Information
Nathaniel V. Nucci. "New insight on the S100A1–STIP1 complex highlights the important relationship between allostery and entropy in protein function" Biochemical Journal Vol. 474 Iss. 17 (2017) p. 2977 - 2980 Available at: http://works.bepress.com/nathaniel-nucci/4/