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EncoMPASS: an online database for analyzing structure and symmetry in membrane proteins.
Sarti, Edoardo; Aleksandrova, Antoniya A; Ganta, Srujan K; Yavatkar, Amarendra S; Forrest, Lucy R.
Affiliation
  • Sarti E; Computational Structural Biology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
  • Aleksandrova AA; Computational Structural Biology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
  • Ganta SK; Bioinformatics Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
  • Yavatkar AS; Bioinformatics Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
  • Forrest LR; Computational Structural Biology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892, USA.
Nucleic Acids Res ; 47(D1): D315-D321, 2019 01 08.
Article in En | MEDLINE | ID: mdl-30357403
The EncoMPASS online database (http://encompass.ninds.nih.gov) collects, organizes, and presents information about membrane proteins of known structure, emphasizing their structural similarities as well as their quaternary and internal symmetries. Unlike, e.g. SCOP, the EncoMPASS database does not aim for a strict classification of membrane proteins, but instead is organized as a protein chain-centric network of sequence and structural homologues. The online server for the EncoMPASS database provides tools for comparing the structural features of its entries, making it a useful resource for homology modeling and active site identification studies. The database can also be used for inferring functionality, which for membrane proteins often involves symmetry-related mechanisms. To this end, the online database also provides a comprehensive description of both the quaternary and internal symmetries in known membrane protein structures, with a particular focus on their orientation relative to the membrane.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Databases, Protein / Membrane Proteins Limits: Animals / Humans Language: En Journal: Nucleic Acids Res Year: 2019 Type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Databases, Protein / Membrane Proteins Limits: Animals / Humans Language: En Journal: Nucleic Acids Res Year: 2019 Type: Article Affiliation country: United States