CoDNaS-Q: a database of conformational diversity of the native state of proteins with quaternary structure

Escobedo N.; Cahui R.R.T.; Caruso G.; Ríos E.G.; Hirsh L.; Monzon A.M.; Parisi G.; Palopoli N. · Bioinformatics (2022) · DOI: 10.1093/bioinformatics/btac627

Resumen

A collection of conformers that exist in a dynamical equilibrium defines the native state of a protein. The structural differences between them describe their conformational diversity, a defining characteristic of the protein with an essential role in multiple cellular processes. Since most proteins carry out their functions by assembling into complexes, we have developed CoDNaS-Q, the first online resource to explore conformational diversity in homooligomeric proteins. It features a curated collection of redundant protein structures with known quaternary structure. CoDNaS-Q integrates relevant annotations that allow researchers to identify and explore the extent and possible reasons of conformational diversity in homooligomeric protein complexes. © The Author(s) 2022. Published by Oxford University Press. All rights reserved.

Instituciones: Pontificia Universidad Católica del Perú