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@article{1206148, author = {Pravda, Lukáš and Berka, Karel and Svobodová Vařeková, Radka and Sehnal, David and Banáš, Pavel and Roman A, Laskowski and Koča, Jaroslav and Otyepka, Michal}, article_location = {England}, article_number = {november}, doi = {http://dx.doi.org/10.1186/s12859-014-0379-x}, keywords = {CATALYTIC SITE ATLAS; ACTIVE-SITE; ION CHANNELS; BIOMACROMOLECULAR CHANNELS; SUBSTRATE PREFERENCES; CYTOCHROMES P450; LIGAND-BINDING; ACCESS TUNNELS; PROTEIN; RESIDUES}, language = {eng}, issn = {1471-2105}, journal = {BMC Bioinformatics}, title = {Anatomy of Enzyme Channels}, url = {http://www.biomedcentral.com/content/pdf/s12859-014-0379-x.pdf}, volume = {15}, year = {2014} }
TY - JOUR ID - 1206148 AU - Pravda, Lukáš - Berka, Karel - Svobodová Vařeková, Radka - Sehnal, David - Banáš, Pavel - Roman A, Laskowski - Koča, Jaroslav - Otyepka, Michal PY - 2014 TI - Anatomy of Enzyme Channels JF - BMC Bioinformatics VL - 15 IS - november SP - "nestránkováno" EP - "nestránkováno" PB - BioMed Central Ltd SN - 14712105 KW - CATALYTIC SITE ATLAS KW - ACTIVE-SITE KW - ION CHANNELS KW - BIOMACROMOLECULAR CHANNELS KW - SUBSTRATE PREFERENCES KW - CYTOCHROMES P450 KW - LIGAND-BINDING KW - ACCESS TUNNELS KW - PROTEIN KW - RESIDUES UR - http://www.biomedcentral.com/content/pdf/s12859-014-0379-x.pdf L2 - http://www.biomedcentral.com/content/pdf/s12859-014-0379-x.pdf N2 - Background: Enzyme active sites can be connected to the exterior environment by one or more channels passing through the protein. Despite our current knowledge of enzyme structure and function, surprisingly little is known about how often channels are present or about any structural features such channels may have in common. Results: Here, we analyze the long channels (i.e. > 15 angstrom) leading to the active sites of 4,306 enzyme structures. We find that over 64% of enzymes contain two or more long channels, their typical length being 28 angstrom. We show that amino acid compositions of the channel significantly differ both to the composition of the active site, surface and interior of the protein. Conclusions: The majority of enzymes have buried active sites accessible via a network of access channels. This indicates that enzymes tend to have buried active sites, with channels controlling access to, and egress from, them, and that suggests channels may play a key role in helping determine enzyme substrate. ER -
PRAVDA, Lukáš, Karel BERKA, Radka SVOBODOVÁ VAŘEKOVÁ, David SEHNAL, Pavel BANÁŠ, Laskowski ROMAN A, Jaroslav KOČA a Michal OTYEPKA. Anatomy of Enzyme Channels. \textit{BMC Bioinformatics}. England: BioMed Central Ltd, 2014, roč.~15, november, s.~''nestránkováno'', 8 s. ISSN~1471-2105. Dostupné z: https://dx.doi.org/10.1186/s12859-014-0379-x.
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