Membranome 2.0: database for proteome-wide profiling of bitopic proteins and their dimers.
Bioinformatics
; 34(6): 1061-1062, 2018 03 15.
Article
em En
| MEDLINE
| ID: mdl-29126305
ABSTRACT
Motivation Structural studies of TM domains of single-spanning (bitopic) membrane proteins are impeded by their instability, flexibility and heterogeneity. The new computational method TMDOCK allows reliable modeling of homodimers of transmembrane (TM) α-helices on a proteomic scale. Results:
3D models of 2129 parallel homodimers formed by TM α-helices of bitopic proteins from six evolutionarily distant organisms were modeled by TMDOCK, verified through experimental data available for nearly 600 proteins, and included in the Membranome database (v.2.0) along with related information to facilitate structural and evolutionary analysis of bitopic proteins. Availability and implementation http//membranome.org. Contact almz@umich.edu. Supplementary information Supplementary data are available at Bioinformatics online.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteoma
/
Multimerização Proteica
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Domínios Proteicos
/
Proteínas de Membrana
Limite:
Humans
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article