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PDBTM: Protein Data Bank of transmembrane proteins after 8 years.


ABSTRACT: The PDBTM database (available at http://pdbtm.enzim.hu), the first comprehensive and up-to-date transmembrane protein selection of the Protein Data Bank, was launched in 2004. The database was created and has been continuously updated by the TMDET algorithm that is able to distinguish between transmembrane and non-transmembrane proteins using their 3D atomic coordinates only. The TMDET algorithm can locate the spatial positions of transmembrane proteins in lipid bilayer as well. During the last 8 years not only the size of the PDBTM database has been steadily growing from ?400 to 1700 entries but also new structural elements have been identified, in addition to the well-known ?-helical bundle and ?-barrel structures. Numerous 'exotic' transmembrane protein structures have been solved since the first release, which has made it necessary to define these new structural elements, such as membrane loops or interfacial helices in the database. This article reports the new features of the PDBTM database that have been added since its first release, and our current efforts to keep the database up-to-date and easy to use so that it may continue to serve as a fundamental resource for the scientific community.

SUBMITTER: Kozma D 

PROVIDER: S-EPMC3531219 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature

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PDBTM: Protein Data Bank of transmembrane proteins after 8 years.

Kozma Dániel D   Simon István I   Tusnády Gábor E GE  

Nucleic acids research 20121130 Database issue


The PDBTM database (available at http://pdbtm.enzim.hu), the first comprehensive and up-to-date transmembrane protein selection of the Protein Data Bank, was launched in 2004. The database was created and has been continuously updated by the TMDET algorithm that is able to distinguish between transmembrane and non-transmembrane proteins using their 3D atomic coordinates only. The TMDET algorithm can locate the spatial positions of transmembrane proteins in lipid bilayer as well. During the last  ...[more]

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