Intrinsic Disorder in Tetratricopeptide Repeat Proteins
Among the realm of repeat containing proteins that commonly serve as “scaffolds” promoting protein-protein interactions, there is a family of proteins containing between 2 and 20 tetratricopeptide repeats (TPRs), which are functional motifs consisting of 34 amino acids. The most distinguishing featu...
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doaj-85cd10f734fa4fcfae3cb81a0d16ef902020-11-25T03:22:58ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-05-01213709370910.3390/ijms21103709Intrinsic Disorder in Tetratricopeptide Repeat ProteinsNathan W. Van Bibber0Cornelia Haerle1Roy Khalife2Bin Xue3Vladimir N. Uversky4. Department of Molecular Medicine Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd., Tampa, FL 33612, USA. Department of Molecular Medicine Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd., Tampa, FL 33612, USA. Department of Molecular Medicine Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd., Tampa, FL 33612, USADepartment of Cell Biology, Microbiology and Molecular Biology, School of Natural Sciences and Mathematics, College of Arts and Sciences, University of South Florida, Tampa, FL 33620, USA. Department of Molecular Medicine Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd., Tampa, FL 33612, USAAmong the realm of repeat containing proteins that commonly serve as “scaffolds” promoting protein-protein interactions, there is a family of proteins containing between 2 and 20 tetratricopeptide repeats (TPRs), which are functional motifs consisting of 34 amino acids. The most distinguishing feature of TPR domains is their ability to stack continuously one upon the other, with these stacked repeats being able to affect interaction with binding partners either sequentially or in combination. It is known that many repeat-containing proteins are characterized by high levels of intrinsic disorder, and that many protein tandem repeats can be intrinsically disordered. Furthermore, it seems that TPR-containing proteins share many characteristics with hybrid proteins containing ordered domains and intrinsically disordered protein regions. However, there has not been a systematic analysis of the intrinsic disorder status of TPR proteins. To fill this gap, we analyzed 166 human TPR proteins to determine the degree to which proteins containing TPR motifs are affected by intrinsic disorder. Our analysis revealed that these proteins are characterized by different levels of intrinsic disorder and contain functional disordered regions that are utilized for protein-protein interactions and often serve as targets of various posttranslational modifications.https://www.mdpi.com/1422-0067/21/10/3709tetratricopeptide repeatintrinsically disordered proteinintrinsically disordered protein regionprotein-protein interactionposttranslational modification |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Nathan W. Van Bibber Cornelia Haerle Roy Khalife Bin Xue Vladimir N. Uversky |
spellingShingle |
Nathan W. Van Bibber Cornelia Haerle Roy Khalife Bin Xue Vladimir N. Uversky Intrinsic Disorder in Tetratricopeptide Repeat Proteins International Journal of Molecular Sciences tetratricopeptide repeat intrinsically disordered protein intrinsically disordered protein region protein-protein interaction posttranslational modification |
author_facet |
Nathan W. Van Bibber Cornelia Haerle Roy Khalife Bin Xue Vladimir N. Uversky |
author_sort |
Nathan W. Van Bibber |
title |
Intrinsic Disorder in Tetratricopeptide Repeat Proteins |
title_short |
Intrinsic Disorder in Tetratricopeptide Repeat Proteins |
title_full |
Intrinsic Disorder in Tetratricopeptide Repeat Proteins |
title_fullStr |
Intrinsic Disorder in Tetratricopeptide Repeat Proteins |
title_full_unstemmed |
Intrinsic Disorder in Tetratricopeptide Repeat Proteins |
title_sort |
intrinsic disorder in tetratricopeptide repeat proteins |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2020-05-01 |
description |
Among the realm of repeat containing proteins that commonly serve as “scaffolds” promoting protein-protein interactions, there is a family of proteins containing between 2 and 20 tetratricopeptide repeats (TPRs), which are functional motifs consisting of 34 amino acids. The most distinguishing feature of TPR domains is their ability to stack continuously one upon the other, with these stacked repeats being able to affect interaction with binding partners either sequentially or in combination. It is known that many repeat-containing proteins are characterized by high levels of intrinsic disorder, and that many protein tandem repeats can be intrinsically disordered. Furthermore, it seems that TPR-containing proteins share many characteristics with hybrid proteins containing ordered domains and intrinsically disordered protein regions. However, there has not been a systematic analysis of the intrinsic disorder status of TPR proteins. To fill this gap, we analyzed 166 human TPR proteins to determine the degree to which proteins containing TPR motifs are affected by intrinsic disorder. Our analysis revealed that these proteins are characterized by different levels of intrinsic disorder and contain functional disordered regions that are utilized for protein-protein interactions and often serve as targets of various posttranslational modifications. |
topic |
tetratricopeptide repeat intrinsically disordered protein intrinsically disordered protein region protein-protein interaction posttranslational modification |
url |
https://www.mdpi.com/1422-0067/21/10/3709 |
work_keys_str_mv |
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