Publicación

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 Monzón · Gustavo Parisi · Nicolás Palópoli

Resumen

SUMMARY: 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. AVAILABILITY AND IMPLEMENTATION: CoDNaS-Q is freely accessible at http://ufq.unq.edu.ar/codnasq/ or https://codnas-q.bioinformatica.org/home. The data can be retrieved from the website. The source code of the database can be downloaded from https://github.com/SfrRonaldo/codnas-q.

Autores y colaboradores

Authors

Nahuel Escobedo
Ronaldo Romario Tunque Cahui
Gastón Caruso
Emilio García Ríos
Alexander Miguel Monzón
Gustavo Parisi
Nicolás Palópoli

Palabras clave

Protein quaternary structure Diversity (politics) Conformational isomerism Protein structure Computer science