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

Nahuel Escobedo, Ronaldo Romario Tunque Cahui, Gastón Caruso, Emilio García Ríos, Layla Hirsh, Alexander Miguel Monzon, Gustavo Parisi, Nicolas Palopoli

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)4959-4961
Number of pages3
JournalBioinformatics
Volume38
Issue number21
DOIs
StatePublished - 1 Nov 2022

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