July 14, 2014
Corresponding author: Peixin Huang huang.peixin@zs-hospital.sh.cn
Hospital, Shanghai 200032, China
Clinical and Translational Medicine 2014, 3:18 doi:10.1186/2001-1326-3-18
Abstract
Allostery is involved in the dynamic regulation of biological functions in proteins. Advances in allostery research have recently drawn great interest and brought allostery closer to the clinic. The present commentary describes the mechanism by which allostery may involve in from a cell-wide view and its contribution to the discovery of new therapeutics to diseases.
Background
Allostery is a universal phenomenon whereby an effector molecule combining with a (allosteric) site on the protein surface leads to a functional change through alteration of shape and/or dynamics, to regulate protein activity. Effector perturbations can result from a wide range of biological and physical phenomena, including the binding of a small effector molecule, post-translational modifications, protein binding, temperature changes, and pH changes. Allostery takes place in all dynamic proteins, single chains, and in RNA and DNA polymers.
The electronic version of this article is the complete one and can be found online at: http://www.clintransmed.com/content/3/1/18
Image source: Bahar Lab
