Email RIS file
Bookmark
Report an Issue

Conformational selection in a protein-protein interaction revealed by dynamic pathway analysis [electronic resource].

Published
Washington, D.C. : United States. Dept. of Energy, 2015.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
Physical Description
pages 32-42 : digital, PDF file
Additional Creators
Brandeis University, United States. Department of Energy, and United States. Department of Energy. Office of Scientific and Technical Information
Access Online

Availability

I Want It
I Want It

Finding items...

Restrictions on Access
Free-to-read Unrestricted online access
Summary
Molecular recognition plays a central role in biology, and protein dynamics has been acknowledged to be important in this process. However, it is highly debated whether conformational changes happen before ligand binding to produce a binding-competent state (conformational selection) or are caused in response to ligand binding (induced fit). Proposals for both mechanisms in protein/protein recognition have been primarily based on structural arguments. However, the distinction between them is a question of the probabilities of going via these two opposing pathways. Here we present a direct demonstration of exclusive conformational selection in protein/protein recognition by measuring the flux for rhodopsin kinase binding to its regulator recoverin, an important molecular recognition in the vision system. Using NMR spectroscopy, stopped-flow kinetics and isothermal titration calorimetry we show that recoverin populates a minor conformation in solution that exposes a hydrophobic binding pocket responsible for binding rhodopsin kinase. Lastly, protein dynamics in free recoverin limits the overall rate of binding.
Report Numbers
E 1.99:1239247
Subject(s)
Other Subject(s)
Note
Published through SciTech Connect.
12/24/2015.
": S2211124715014230"
Cell Reports 14 1 ISSN 2211-1247 AM
Kalyan S. Chakrabarti; Roman V. Agafonov; Francesco Pontiggia; Renee Otten; Matthew K. Higgins; Gebhard F. X. Schertler; Daniel D. Oprian; Dorothee Kern.
Funding Information
FG02-05ER15699
View MARC record | catkey: 23500263