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Membranome 3.0: Database of single-pass membrane proteins with AlphaFold models.
Lomize, Andrei L; Schnitzer, Kevin A; Todd, Spencer C; Cherepanov, Stanislav; Outeiral, Carlos; Deane, Charlotte M; Pogozheva, Irina D.
Afiliação
  • Lomize AL; Department of Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan, USA.
  • Schnitzer KA; Department of Electrical Engineering and Computer Science, College of Engineering, University of Michigan, Ann Arbor, Michigan, USA.
  • Todd SC; Department of Electrical Engineering and Computer Science, College of Engineering, University of Michigan, Ann Arbor, Michigan, USA.
  • Cherepanov S; Department of Biophysics, University of Michigan, Ann Arbor, Michigan, USA.
  • Outeiral C; Department of Statistics, University of Oxford, UK.
  • Deane CM; Department of Statistics, University of Oxford, UK.
  • Pogozheva ID; Department of Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, Michigan, USA.
Protein Sci ; 31(5): e4318, 2022 05.
Article em En | MEDLINE | ID: mdl-35481632
ABSTRACT
The Membranome database provides comprehensive structural information on single-pass (i.e., bitopic) membrane proteins from six evolutionarily distant organisms, including protein-protein interactions, complexes, mutations, experimental structures, and models of transmembrane α-helical dimers. We present a new version of this database, Membranome 3.0, which was significantly updated by revising the set of 5,758 bitopic proteins and incorporating models generated by AlphaFold 2 in the database. The AlphaFold models were parsed into structural domains located at the different membrane sides, modified to exclude low-confidence unstructured terminal regions and signal sequences, validated through comparison with available experimental structures, and positioned with respect to membrane boundaries. Membranome 3.0 was re-developed to facilitate visualization and comparative analysis of multiple 3D structures of proteins that belong to a specified family, complex, biological pathway, or membrane type. New tools for advanced search and analysis of proteins, their interactions, complexes, and mutations were included. The database is freely accessible at https//membranome.org.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Membrana Idioma: En Revista: Protein Sci Assunto da revista: BIOQUIMICA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Membrana Idioma: En Revista: Protein Sci Assunto da revista: BIOQUIMICA Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Estados Unidos