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Transmembrane Protein Docking with JabberDock
[Image: see text] Transmembrane proteins act as an intermediary for a broad range of biological process. Making up 20% to 30% of the proteome, their ubiquitous nature has resulted in them comprising 50% of all targets in drug design. Despite their importance, they make up only 4% of all structures i...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8041277/ https://www.ncbi.nlm.nih.gov/pubmed/33635637 http://dx.doi.org/10.1021/acs.jcim.0c01315 |
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author | Rudden, Lucas S. P. Degiacomi, Matteo T. |
author_facet | Rudden, Lucas S. P. Degiacomi, Matteo T. |
author_sort | Rudden, Lucas S. P. |
collection | PubMed |
description | [Image: see text] Transmembrane proteins act as an intermediary for a broad range of biological process. Making up 20% to 30% of the proteome, their ubiquitous nature has resulted in them comprising 50% of all targets in drug design. Despite their importance, they make up only 4% of all structures in the PDB database, primarily owing to difficulties associated with isolating and characterizing them. Membrane protein docking algorithms could help to fill this knowledge gap, yet only few exist. Moreover, these existing methods achieve success rates lower than the current best soluble proteins docking software. We present and test a pipeline using our software, JabberDock, to dock membrane proteins. JabberDock docks shapes representative of membrane protein structure and dynamics in their biphasic environment. We verify JabberDock’s ability to yield accurate predictions by applying it to a benchmark of 20 transmembrane dimers, returning a success rate of 75.0%. This makes our software very competitive among available membrane protein–protein docking tools. |
format | Online Article Text |
id | pubmed-8041277 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-80412772021-04-13 Transmembrane Protein Docking with JabberDock Rudden, Lucas S. P. Degiacomi, Matteo T. J Chem Inf Model [Image: see text] Transmembrane proteins act as an intermediary for a broad range of biological process. Making up 20% to 30% of the proteome, their ubiquitous nature has resulted in them comprising 50% of all targets in drug design. Despite their importance, they make up only 4% of all structures in the PDB database, primarily owing to difficulties associated with isolating and characterizing them. Membrane protein docking algorithms could help to fill this knowledge gap, yet only few exist. Moreover, these existing methods achieve success rates lower than the current best soluble proteins docking software. We present and test a pipeline using our software, JabberDock, to dock membrane proteins. JabberDock docks shapes representative of membrane protein structure and dynamics in their biphasic environment. We verify JabberDock’s ability to yield accurate predictions by applying it to a benchmark of 20 transmembrane dimers, returning a success rate of 75.0%. This makes our software very competitive among available membrane protein–protein docking tools. American Chemical Society 2021-02-26 2021-03-22 /pmc/articles/PMC8041277/ /pubmed/33635637 http://dx.doi.org/10.1021/acs.jcim.0c01315 Text en © 2021 American Chemical Society Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Rudden, Lucas S. P. Degiacomi, Matteo T. Transmembrane Protein Docking with JabberDock |
title | Transmembrane Protein Docking with JabberDock |
title_full | Transmembrane Protein Docking with JabberDock |
title_fullStr | Transmembrane Protein Docking with JabberDock |
title_full_unstemmed | Transmembrane Protein Docking with JabberDock |
title_short | Transmembrane Protein Docking with JabberDock |
title_sort | transmembrane protein docking with jabberdock |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8041277/ https://www.ncbi.nlm.nih.gov/pubmed/33635637 http://dx.doi.org/10.1021/acs.jcim.0c01315 |
work_keys_str_mv | AT ruddenlucassp transmembraneproteindockingwithjabberdock AT degiacomimatteot transmembraneproteindockingwithjabberdock |