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

Bioinformatics. 2022 Sep 16:btac627. doi: 10.1093/bioinformatics/btac627. Online ahead of print.

ABSTRACT

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.

SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.

PMID:36111870 | DOI:10.1093/bioinformatics/btac627