Informace o publikaci

Secondary Structure Elements-Annotations and Schematic 2D Visualizations Stable for Individual Protein Families

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SVOBODOVÁ VAŘEKOVÁ Radka MIDLIK Adam HUTAŘOVÁ VAŘEKOVÁ Ivana HUTAŘ Jan NAVRÁTILOVÁ Veronika KOČA Jaroslav BERKA Karel

Rok publikování 2018
Druh Konferenční abstrakty
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
Popis Composition and organization of secondary structure elements (SSEs), such as alpha-helices and beta-sheets, are characteristic for protein families and they participate in formation of protein fold. They are however often influenced by the sequence variability and ligand binding. For this reason, identification of similarities and differences between SSEs can help us in the analysis of individual proteins within a protein family. To utilize the SSEs for research of individual protein families, we need to have the SSEs easily and automatically intercomparable within one protein family. Specifically, the corresponding SSEs should have the same name (annotation) and there should be a transparent schema of their localization in the protein structures. Unfortunately, SSE annotations are still performed mainly manually and universal automatic approach to assign SSE names is not available yet. Moreover, current methods focused on 2D visualization of SSEs (e.g., PROMOTIF, Pro-origami, HERA) do not consider information about real distances of SSEs. Therefore, even when two proteins from the same family differ only slightly, their SSE 2D diagrams can be totally different. For this reason, we developed a tool set which can perform SSE annotation and 2D visualization in such a way that structural information is kept. Applicability of this approach is shown in a case study focused on cytochromes P450. This protein family of drug-metabolizing enzymes has currently available more than 750 structures from about 30 organisms and each cytochrome P450 contains more than 20 SSEs for which there is a stable annotation used through the community. Our approach can be further extended to other protein structural families, which will allow family-wide SSE annotations and comparisons in a simple visual manner.
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