| URL: | http://ufq.unq.edu.ar/codnasq |
| Full name: | a database of conformational diversity of the native state of proteins with quaternary structure |
| Description: | CoDNaS-Q integrates relevant annotations that allow researchers to identify and explore the extent and possible reasons of conformational diversity in homooligomeric protein complexes |
| Year founded: | 2022 |
| Last update: | 2022-10-31 |
| Version: | 1.0 |
| Accessibility: |
Accessible
|
| Country/Region: | Argentina |
| Data type: | |
| Data object: |
NA
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| Database category: | |
| Major species: |
NA
|
| Keywords: |
| University/Institution: | Universidad Nacional de Quilmes |
| Address: | Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, Buenos Aires B1876BXD, Argentina. |
| City: | |
| Province/State: | |
| Country/Region: | Argentina |
| Contact name (PI/Team): | Nicolas Palopoli |
| Contact email (PI/Helpdesk): | npalopoli@unq.edu.ar |
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CoDNaS-Q: a database of conformational diversity of the native state of proteins with quaternary structure. [PMID: 36111870]
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. |