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Database (Oxford) ; 2024: 0, 2024 Aug 08.
Artículo en Inglés | MEDLINE | ID: mdl-39126203

RESUMEN

A structural alteration in copper/zinc superoxide dismutase (SOD1) is one of the common features caused by amyotrophic lateral sclerosis (ALS)-linked mutations. Although a large number of SOD1 variants have been reported in ALS patients, the detailed structural properties of each variant are not well summarized. We present SoDCoD, a database of superoxide dismutase conformational diversity, collecting our comprehensive biochemical analyses of the structural changes in SOD1 caused by ALS-linked gene mutations and other perturbations. SoDCoD version 1.0 contains information about the properties of 188 types of SOD1 mutants, including structural changes and their binding to Derlin-1, as well as a set of genes contributing to the proteostasis of mutant-like wild-type SOD1. This database provides valuable insights into the diagnosis and treatment of ALS, particularly by targeting conformational alterations in SOD1. Database URL: https://fujisawagroup.github.io/SoDCoDweb/.


Asunto(s)
Esclerosis Amiotrófica Lateral , Mutación , Superóxido Dismutasa-1 , Esclerosis Amiotrófica Lateral/genética , Esclerosis Amiotrófica Lateral/enzimología , Humanos , Superóxido Dismutasa-1/genética , Superóxido Dismutasa-1/química , Superóxido Dismutasa-1/metabolismo , Bases de Datos de Proteínas , Conformación Proteica , Bases de Datos Genéticas , Superóxido Dismutasa/genética , Superóxido Dismutasa/química , Superóxido Dismutasa/metabolismo
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