Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl <i>cis/trans</i> Isomerases (PPIase)
In this technical note, we describe analyses of more than 15,000 sequences of FK506-binding proteins (FKBP) and cyclophilins, also known as peptidyl-prolyl <i>cis/trans</i> isomerases (PPIases). We have developed a novel way of displaying relative changes of amino acid (AA)-residues at a...
| Main Author: | |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2019-02-01
|
| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/9/2/59 |
| _version_ | 1811239876598693888 |
|---|---|
| author | Andrzej Galat |
| author_facet | Andrzej Galat |
| author_sort | Andrzej Galat |
| collection | DOAJ |
| description | In this technical note, we describe analyses of more than 15,000 sequences of FK506-binding proteins (FKBP) and cyclophilins, also known as peptidyl-prolyl <i>cis/trans</i> isomerases (PPIases). We have developed a novel way of displaying relative changes of amino acid (AA)-residues at a given sequence position by using heat-maps. This type of representation allows simultaneous estimation of conservation level in a given sequence position in the entire group of functionally-related paralogues (multigene family of proteins). We have also proposed that at least two FKBPs, namely FKBP36, encoded by the <i>Fkbp6</i> gene and FKBP51, encoded by the <i>Fkbp5</i> gene, can form dimers bound via a disulfide bridge in the nucleus. This type of dimer may have some crucial function in the regulation of some nuclear complexes at different stages of the cell cycle. |
| first_indexed | 2024-04-12T13:08:56Z |
| format | Article |
| id | doaj.art-159538741bae436e80c6904483692a6e |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-04-12T13:08:56Z |
| publishDate | 2019-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-159538741bae436e80c6904483692a6e2022-12-22T03:31:54ZengMDPI AGBiomolecules2218-273X2019-02-01925910.3390/biom9020059biom9020059Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl <i>cis/trans</i> Isomerases (PPIase)Andrzej Galat0Service d’Ingénierie Moléculaire des Protéines (SIMOPRO), CEA-Université Paris-Saclay, F-91191 Gif/Yvette, FranceIn this technical note, we describe analyses of more than 15,000 sequences of FK506-binding proteins (FKBP) and cyclophilins, also known as peptidyl-prolyl <i>cis/trans</i> isomerases (PPIases). We have developed a novel way of displaying relative changes of amino acid (AA)-residues at a given sequence position by using heat-maps. This type of representation allows simultaneous estimation of conservation level in a given sequence position in the entire group of functionally-related paralogues (multigene family of proteins). We have also proposed that at least two FKBPs, namely FKBP36, encoded by the <i>Fkbp6</i> gene and FKBP51, encoded by the <i>Fkbp5</i> gene, can form dimers bound via a disulfide bridge in the nucleus. This type of dimer may have some crucial function in the regulation of some nuclear complexes at different stages of the cell cycle.https://www.mdpi.com/2218-273X/9/2/59FKBPcyclophilinPPIaseheat-mapimmunophilin |
| spellingShingle | Andrzej Galat Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl <i>cis/trans</i> Isomerases (PPIase) Biomolecules FKBP cyclophilin PPIase heat-map immunophilin |
| title | Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl <i>cis/trans</i> Isomerases (PPIase) |
| title_full | Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl <i>cis/trans</i> Isomerases (PPIase) |
| title_fullStr | Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl <i>cis/trans</i> Isomerases (PPIase) |
| title_full_unstemmed | Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl <i>cis/trans</i> Isomerases (PPIase) |
| title_short | Compression of Large Sets of Sequence Data Reveals Fine Diversification of Functional Profiles in Multigene Families of Proteins: A Study for Peptidyl-Prolyl <i>cis/trans</i> Isomerases (PPIase) |
| title_sort | compression of large sets of sequence data reveals fine diversification of functional profiles in multigene families of proteins a study for peptidyl prolyl i cis trans i isomerases ppiase |
| topic | FKBP cyclophilin PPIase heat-map immunophilin |
| url | https://www.mdpi.com/2218-273X/9/2/59 |
| work_keys_str_mv | AT andrzejgalat compressionoflargesetsofsequencedatarevealsfinediversificationoffunctionalprofilesinmultigenefamiliesofproteinsastudyforpeptidylprolylicistransiisomerasesppiase |