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

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Oxford University Press

Acceso al texto completo solo para la Comunidad PUCP

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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.

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Protein quaternary structure, Diversity (politics), Conformational isomerism, Protein structure, Computer science, Functional diversity, Source code, Computational biology, Resource (disambiguation), Database, Biology, Chemistry, Programming language, Biochemistry, Molecule

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