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.
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CITATION STYLE
Escobedo, N., Cahui, R. R. T., Caruso, G., Ríos, E. G., Hirsh, L., Monzon, A. M., … Palopoli, N. (2022). CoDNaS-Q: a database of conformational diversity of the native state of proteins with quaternary structure. Bioinformatics, 38(21), 4959–4961. https://doi.org/10.1093/bioinformatics/btac627
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