Cargando…
TSTMP: target selection for structural genomics of human transmembrane proteins
The TSTMP database is designed to help the target selection of human transmembrane proteins for structural genomics projects and structure modeling studies. Currently, there are only 60 known 3D structures among the polytopic human transmembrane proteins and about a further 600 could be modeled usin...
Autores principales: | , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5210638/ https://www.ncbi.nlm.nih.gov/pubmed/27924015 http://dx.doi.org/10.1093/nar/gkw939 |
_version_ | 1782490925100957696 |
---|---|
author | Varga, Julia Dobson, László Reményi, István Tusnády, Gábor E. |
author_facet | Varga, Julia Dobson, László Reményi, István Tusnády, Gábor E. |
author_sort | Varga, Julia |
collection | PubMed |
description | The TSTMP database is designed to help the target selection of human transmembrane proteins for structural genomics projects and structure modeling studies. Currently, there are only 60 known 3D structures among the polytopic human transmembrane proteins and about a further 600 could be modeled using existing structures. Although there are a great number of human transmembrane protein structures left to be determined, surprisingly only a small fraction of these proteins have ‘selected’ (or above) status according to the current version the TargetDB/TargetTrack database. This figure is even worse regarding those transmembrane proteins that would contribute the most to the structural coverage of the human transmembrane proteome. The database was built by sorting out proteins from the human transmembrane proteome with known structure and searching for suitable model structures for the remaining proteins by combining the results of a state-of-the-art transmembrane specific fold recognition algorithm and a sequence similarity search algorithm. Proteins were searched for homologues among the human transmembrane proteins in order to select targets whose successful structure determination would lead to the best structural coverage of the human transmembrane proteome. The pipeline constructed for creating the TSTMP database guarantees to keep the database up-to-date. The database is available at http://tstmp.enzim.ttk.mta.hu. |
format | Online Article Text |
id | pubmed-5210638 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-52106382017-01-05 TSTMP: target selection for structural genomics of human transmembrane proteins Varga, Julia Dobson, László Reményi, István Tusnády, Gábor E. Nucleic Acids Res Database Issue The TSTMP database is designed to help the target selection of human transmembrane proteins for structural genomics projects and structure modeling studies. Currently, there are only 60 known 3D structures among the polytopic human transmembrane proteins and about a further 600 could be modeled using existing structures. Although there are a great number of human transmembrane protein structures left to be determined, surprisingly only a small fraction of these proteins have ‘selected’ (or above) status according to the current version the TargetDB/TargetTrack database. This figure is even worse regarding those transmembrane proteins that would contribute the most to the structural coverage of the human transmembrane proteome. The database was built by sorting out proteins from the human transmembrane proteome with known structure and searching for suitable model structures for the remaining proteins by combining the results of a state-of-the-art transmembrane specific fold recognition algorithm and a sequence similarity search algorithm. Proteins were searched for homologues among the human transmembrane proteins in order to select targets whose successful structure determination would lead to the best structural coverage of the human transmembrane proteome. The pipeline constructed for creating the TSTMP database guarantees to keep the database up-to-date. The database is available at http://tstmp.enzim.ttk.mta.hu. Oxford University Press 2017-01-04 2016-10-18 /pmc/articles/PMC5210638/ /pubmed/27924015 http://dx.doi.org/10.1093/nar/gkw939 Text en © The Author(s) 2016. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Database Issue Varga, Julia Dobson, László Reményi, István Tusnády, Gábor E. TSTMP: target selection for structural genomics of human transmembrane proteins |
title | TSTMP: target selection for structural genomics of human transmembrane proteins |
title_full | TSTMP: target selection for structural genomics of human transmembrane proteins |
title_fullStr | TSTMP: target selection for structural genomics of human transmembrane proteins |
title_full_unstemmed | TSTMP: target selection for structural genomics of human transmembrane proteins |
title_short | TSTMP: target selection for structural genomics of human transmembrane proteins |
title_sort | tstmp: target selection for structural genomics of human transmembrane proteins |
topic | Database Issue |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5210638/ https://www.ncbi.nlm.nih.gov/pubmed/27924015 http://dx.doi.org/10.1093/nar/gkw939 |
work_keys_str_mv | AT vargajulia tstmptargetselectionforstructuralgenomicsofhumantransmembraneproteins AT dobsonlaszlo tstmptargetselectionforstructuralgenomicsofhumantransmembraneproteins AT remenyiistvan tstmptargetselectionforstructuralgenomicsofhumantransmembraneproteins AT tusnadygabore tstmptargetselectionforstructuralgenomicsofhumantransmembraneproteins |