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Structure-Based Characterization of Multiprotein Complexes

Multiprotein complexes govern virtually all cellular processes. Their 3D structures provide important clues to their biological roles, especially through structural correlations among protein molecules and complexes. The detection of such correlations generally requires comprehensive searches in dat...

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Detalles Bibliográficos
Autores principales: Wiederstein, Markus, Gruber, Markus, Frank, Karl, Melo, Francisco, Sippl, Manfred J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4087271/
https://www.ncbi.nlm.nih.gov/pubmed/24954616
http://dx.doi.org/10.1016/j.str.2014.05.005
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author Wiederstein, Markus
Gruber, Markus
Frank, Karl
Melo, Francisco
Sippl, Manfred J.
author_facet Wiederstein, Markus
Gruber, Markus
Frank, Karl
Melo, Francisco
Sippl, Manfred J.
author_sort Wiederstein, Markus
collection PubMed
description Multiprotein complexes govern virtually all cellular processes. Their 3D structures provide important clues to their biological roles, especially through structural correlations among protein molecules and complexes. The detection of such correlations generally requires comprehensive searches in databases of known protein structures by means of appropriate structure-matching techniques. Here, we present a high-speed structure search engine capable of instantly matching large protein oligomers against the complete and up-to-date database of biologically functional assemblies of protein molecules. We use this tool to reveal unseen structural correlations on the level of protein quaternary structure and demonstrate its general usefulness for efficiently exploring complex structural relationships among known protein assemblies.
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spelling pubmed-40872712014-07-10 Structure-Based Characterization of Multiprotein Complexes Wiederstein, Markus Gruber, Markus Frank, Karl Melo, Francisco Sippl, Manfred J. Structure Resource Multiprotein complexes govern virtually all cellular processes. Their 3D structures provide important clues to their biological roles, especially through structural correlations among protein molecules and complexes. The detection of such correlations generally requires comprehensive searches in databases of known protein structures by means of appropriate structure-matching techniques. Here, we present a high-speed structure search engine capable of instantly matching large protein oligomers against the complete and up-to-date database of biologically functional assemblies of protein molecules. We use this tool to reveal unseen structural correlations on the level of protein quaternary structure and demonstrate its general usefulness for efficiently exploring complex structural relationships among known protein assemblies. Cell Press 2014-07-08 /pmc/articles/PMC4087271/ /pubmed/24954616 http://dx.doi.org/10.1016/j.str.2014.05.005 Text en © 2014 The Authors http://creativecommons.org/licenses/by-nc-sa/3.0/ This is an open access article under the CC BY-NC-SA license (http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Resource
Wiederstein, Markus
Gruber, Markus
Frank, Karl
Melo, Francisco
Sippl, Manfred J.
Structure-Based Characterization of Multiprotein Complexes
title Structure-Based Characterization of Multiprotein Complexes
title_full Structure-Based Characterization of Multiprotein Complexes
title_fullStr Structure-Based Characterization of Multiprotein Complexes
title_full_unstemmed Structure-Based Characterization of Multiprotein Complexes
title_short Structure-Based Characterization of Multiprotein Complexes
title_sort structure-based characterization of multiprotein complexes
topic Resource
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4087271/
https://www.ncbi.nlm.nih.gov/pubmed/24954616
http://dx.doi.org/10.1016/j.str.2014.05.005
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