Cytochrome P450 structure anatomy – recognition and analysis of
secondary structure elements

a 2017

Cytochrome P450 structure anatomy – recognition and analysis of secondary structure elements

MIDLIK, Adam, Radka SVOBODOVÁ VAŘEKOVÁ, Veronika NAVRÁTILOVÁ, Karel BERKA, Jaroslav KOČA et. al.

Základní údaje

Originální název

Cytochrome P450 structure anatomy – recognition and analysis of secondary structure elements

Autoři

MIDLIK, Adam, Radka SVOBODOVÁ VAŘEKOVÁ, Veronika NAVRÁTILOVÁ, Karel BERKA a Jaroslav KOČA

Vydání

ISMB/ECCB, Prague, 2017

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Organizační jednotka

Přírodovědecká fakulta

Příznaky

Mezinárodní význam

Změněno: 22. 1. 2020 13:41, Mgr. et Mgr. Adam Midlik, Ph.D.

Anotace

V originále

Nowadays, structural bioinformatics faces an enormous growth in the number of available protein structures. Moreover, structurally similar proteins form protein families and these families represent rich datasets. In order to understand their molecular function we must focus on the key structural regions (binding sites, channels, allosteric sites, etc.), which involve both conserved and variable regions. Number and position of secondary structure elements (helices and sheets) is usually highly conserved within each protein family, thus they can serve as a firm point for identification of these key regions. Cytochromes P450 are proteins responsible for degradation of drugs and other xenobiotic substances in the organism and thus understanding of their function is crucial in drug design. They are an example of a protein family where the secondary structure elements are traditionally annotated with fixed names, facilitating description and comparison of their structures in the literature. In the last few years, the number of resolved cytochrome P450 structures has grown markedly and currently there are available more than 700 structures originating from more than 50 different organisms. Conserved annotation motivated us to analyze secondary structure elements across the whole cytochrome P450 family. During this process, we first developed an algorithm for automated annotation of secondary structure elements based on a template protein annotation. Secondly, we described the general anatomy and variability of cytochromes P450, based on this annotation. Specifically, we report features of their secondary structure elements such as frequency of occurrence, typical length, amino acid composition, and relation to the source organism.

Citovat

MIDLIK, Adam, Radka SVOBODOVÁ VAŘEKOVÁ, Veronika NAVRÁTILOVÁ, Karel BERKA a Jaroslav KOČA. Cytochrome P450 structure anatomy – recognition and analysis of secondary structure elements. In ISMB/ECCB, Prague. 2017.

@proceedings{1608522,
   author = {Midlik, Adam and Svobodová Vařeková, Radka and Navrátilová, Veronika and Berka, Karel and Koča, Jaroslav},
   booktitle = {ISMB/ECCB, Prague},
   language = {eng},
   title = {Cytochrome P450 structure anatomy – recognition and analysis of secondary structure elements},
   url = {https://www.iscb.org/ismbeccb2017},
   year = {2017}
}

TY  - CONF
ID  - 1608522
AU  - Midlik, Adam - Svobodová Vařeková, Radka - Navrátilová, Veronika - Berka, Karel - Koča, Jaroslav
PY  - 2017
TI  - Cytochrome P450 structure anatomy – recognition and analysis of secondary structure elements
UR  - https://www.iscb.org/ismbeccb2017
N2  - Nowadays, structural bioinformatics faces an enormous growth in the number of available protein structures. Moreover, structurally similar proteins form protein families and these families represent rich datasets. In order to understand their molecular function we must focus on the key structural regions (binding sites, channels, allosteric sites, etc.), which involve both conserved and variable regions. Number and position of secondary structure elements (helices and sheets) is usually highly conserved within each protein family, thus they can serve as a firm point for identification of these key regions. Cytochromes P450 are proteins responsible for degradation of drugs and other xenobiotic substances in the organism and thus understanding of their function is crucial in drug design. They are an example of a protein family where the secondary structure elements are traditionally annotated with fixed names, facilitating description and comparison of their structures in the literature. In the last few years, the number of resolved cytochrome P450 structures has grown markedly and currently there are available more than 700 structures originating from more than 50 different organisms. Conserved annotation motivated us to analyze secondary structure elements across the whole cytochrome P450 family. During this process, we first developed an algorithm for automated annotation of secondary structure elements based on a template protein annotation. Secondly, we described the general anatomy and variability of cytochromes P450, based on this annotation. Specifically, we report features of their secondary structure elements such as frequency of occurrence, typical length, amino acid composition, and relation to the source organism.
ER  -

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