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

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

4 Citas (Scopus)

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.

Idioma originalInglés
Páginas (desde-hasta)4959-4961
Número de páginas3
PublicaciónBioinformatics
Volumen38
N.º21
DOI
EstadoPublicada - 1 nov. 2022

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