Anatomy of Enzyme Channels

Logo poskytovatele

Varování

Publikace nespadá pod Ústav výpočetní techniky, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.
Autoři

PRAVDA Lukáš BERKA Karel SVOBODOVÁ VAŘEKOVÁ Radka SEHNAL David BANÁŠ Pavel ROMAN A Laskowski KOČA Jaroslav OTYEPKA Michal

Rok publikování 2014
Druh Článek v odborném periodiku
Časopis / Zdroj BMC Bioinformatics
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
www http://www.biomedcentral.com/content/pdf/s12859-014-0379-x.pdf
Doi http://dx.doi.org/10.1186/s12859-014-0379-x
Obor Biochemie
Klíčová slova CATALYTIC SITE ATLAS; ACTIVE-SITE; ION CHANNELS; BIOMACROMOLECULAR CHANNELS; SUBSTRATE PREFERENCES; CYTOCHROMES P450; LIGAND-BINDING; ACCESS TUNNELS; PROTEIN; RESIDUES
Popis 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.
Související projekty:

Používáte starou verzi internetového prohlížeče. Doporučujeme aktualizovat Váš prohlížeč na nejnovější verzi.

Další info