Library of disordered patterns in 3D protein structures.

Intrinsically disordered regions serve as molecular recognition elements, which play an important role in the control of many cellular processes and signaling pathways. It is useful to be able to predict positions of disordered regions in protein chains. The statistical analysis of disordered residu...

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Autores principales:	Michail Yu Lobanov, Eugeniya I Furletova, Natalya S Bogatyreva, Michail A Roytberg, Oxana V Galzitskaya
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/594576c712fd4b48bf67b8b707db5a19
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spelling	oai:doaj.org-article:594576c712fd4b48bf67b8b707db5a192021-11-18T05:50:54ZLibrary of disordered patterns in 3D protein structures.1553-734X1553-735810.1371/journal.pcbi.1000958https://doaj.org/article/594576c712fd4b48bf67b8b707db5a192010-10-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20976197/?tool=EBIhttps://doaj.org/toc/1553-734Xhttps://doaj.org/toc/1553-7358Intrinsically disordered regions serve as molecular recognition elements, which play an important role in the control of many cellular processes and signaling pathways. It is useful to be able to predict positions of disordered regions in protein chains. The statistical analysis of disordered residues was done considering 34,464 unique protein chains taken from the PDB database. In this database, 4.95% of residues are disordered (i.e. invisible in X-ray structures). The statistics were obtained separately for the N- and C-termini as well as for the central part of the protein chain. It has been shown that frequencies of occurrence of disordered residues of 20 types at the termini of protein chains differ from the ones in the middle part of the protein chain. Our systematic analysis of disordered regions in PDB revealed 109 disordered patterns of different lengths. Each of them has disordered occurrences in at least five protein chains with identity less than 20%. The vast majority of all occurrences of each disordered pattern are disordered. This allows one to use the library of disordered patterns for predicting the status of a residue of a given protein to be ordered or disordered. We analyzed the occurrence of the selected patterns in three eukaryotic and three bacterial proteomes.Michail Yu LobanovEugeniya I FurletovaNatalya S BogatyrevaMichail A RoytbergOxana V GalzitskayaPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Computational Biology, Vol 6, Iss 10, p e1000958 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Michail Yu Lobanov Eugeniya I Furletova Natalya S Bogatyreva Michail A Roytberg Oxana V Galzitskaya Library of disordered patterns in 3D protein structures.
description	Intrinsically disordered regions serve as molecular recognition elements, which play an important role in the control of many cellular processes and signaling pathways. It is useful to be able to predict positions of disordered regions in protein chains. The statistical analysis of disordered residues was done considering 34,464 unique protein chains taken from the PDB database. In this database, 4.95% of residues are disordered (i.e. invisible in X-ray structures). The statistics were obtained separately for the N- and C-termini as well as for the central part of the protein chain. It has been shown that frequencies of occurrence of disordered residues of 20 types at the termini of protein chains differ from the ones in the middle part of the protein chain. Our systematic analysis of disordered regions in PDB revealed 109 disordered patterns of different lengths. Each of them has disordered occurrences in at least five protein chains with identity less than 20%. The vast majority of all occurrences of each disordered pattern are disordered. This allows one to use the library of disordered patterns for predicting the status of a residue of a given protein to be ordered or disordered. We analyzed the occurrence of the selected patterns in three eukaryotic and three bacterial proteomes.
format	article
author	Michail Yu Lobanov Eugeniya I Furletova Natalya S Bogatyreva Michail A Roytberg Oxana V Galzitskaya
author_facet	Michail Yu Lobanov Eugeniya I Furletova Natalya S Bogatyreva Michail A Roytberg Oxana V Galzitskaya
author_sort	Michail Yu Lobanov
title	Library of disordered patterns in 3D protein structures.
title_short	Library of disordered patterns in 3D protein structures.
title_full	Library of disordered patterns in 3D protein structures.
title_fullStr	Library of disordered patterns in 3D protein structures.
title_full_unstemmed	Library of disordered patterns in 3D protein structures.
title_sort	library of disordered patterns in 3d protein structures.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/594576c712fd4b48bf67b8b707db5a19
work_keys_str_mv	AT michailyulobanov libraryofdisorderedpatternsin3dproteinstructures AT eugeniyaifurletova libraryofdisorderedpatternsin3dproteinstructures AT natalyasbogatyreva libraryofdisorderedpatternsin3dproteinstructures AT michailaroytberg libraryofdisorderedpatternsin3dproteinstructures AT oxanavgalzitskaya libraryofdisorderedpatternsin3dproteinstructures
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Library of disordered patterns in 3D protein structures.

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