Enrico Guarnera1, Zhen Wah Tan1, Zejun Zheng1, Igor N Berezovsky1,2. 1. Bioinformatics Institute (BII), Agency for Science, Technology and Research (A*STAR), Singapore 138671, Singapore. 2. Department of Biological Sciences (DBS), National University of Singapore (NUS), Singapore 117597, Singapore.
Abstract
MOTIVATION: Allostery is an omnipresent mechanism of the function modulation in proteins via either effector binding or mutations in the exosites. Despite the growing number of online servers and databases devoted to prediction/classification of allosteric sites and their characteristics, there is a lack of resources for an efficient and quick estimation of the causality and energetics of allosteric communication. RESULTS: The AlloSigMA server implements a unique approach on the basis of the recently introduced structure-based statistical mechanical models of allosteric signaling. It provides an interactive framework for estimating the allosteric free energy as a result of the ligand(s) binding, mutation(s) and their combinations. Latent regulatory exosites and allosteric effect of mutations can be detected and explored, facilitating the research efforts in protein engineering and allosteric drug design. AVAILABILITY AND IMPLEMENTATION: The AlloSigMA server is freely available at http://allosigma.bii.a-star.edu.sg/home/. CONTACT: igorb@bii.a-star.edu.sg.
MOTIVATION: Allostery is an omnipresent mechanism of the function modulation in proteins via either effector binding or mutations in the exosites. Despite the growing number of online servers and databases devoted to prediction/classification of allosteric sites and their characteristics, there is a lack of resources for an efficient and quick estimation of the causality and energetics of allosteric communication. RESULTS: The AlloSigMA server implements a unique approach on the basis of the recently introduced structure-based statistical mechanical models of allosteric signaling. It provides an interactive framework for estimating the allosteric free energy as a result of the ligand(s) binding, mutation(s) and their combinations. Latent regulatory exosites and allosteric effect of mutations can be detected and explored, facilitating the research efforts in protein engineering and allosteric drug design. AVAILABILITY AND IMPLEMENTATION: The AlloSigMA server is freely available at http://allosigma.bii.a-star.edu.sg/home/. CONTACT: igorb@bii.a-star.edu.sg.
Authors: Giancarlo Abis; Rebecca L Charles; Jolanta Kopec; Wyatt W Yue; R Andrew Atkinson; Tam T T Bui; Steven Lynham; Simona Popova; Yin-Biao Sun; Franca Fraternali; Philip Eaton; Maria R Conte Journal: Commun Biol Date: 2019-05-17
Authors: Jian Wang; Abha Jain; Leanna R McDonald; Craig Gambogi; Andrew L Lee; Nikolay V Dokholyan Journal: Nat Commun Date: 2020-07-31 Impact factor: 14.919