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Volume 12
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10.3390/biom12081098
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Article

Low Complexity Induces Structure in Protein Regions Predicted as Intrinsically Disordered

by
Mariane Gonçalves-Kulik
1,
Pablo Mier
1,
Kristina Kastano
1,
Juan Cortés
2,
Pau Bernadó
3,
Friederike Schmid
4 and
Miguel A. Andrade-Navarro
1,*
1
Institute of Organismic and Molecular Evolution, Faculty of Biology, Johannes Gutenberg University of Mainz, 55128 Mainz, Germany
2
LAAS-CNRS, Université de Toulouse, CNRS, 31400 Toulouse, France
3
Centre de Biologie Structurale (CBS), Université de Montpellier INSERM, CNRS, 34090 Montpellier, France
4
Faculty of Physics, Johannes Gutenberg University of Mainz, 55128 Mainz, Germany
*
Author to whom correspondence should be addressed.
Biomolecules 2022, 12(8), 1098; https://doi.org/10.3390/biom12081098
Submission received: 15 June 2022 / Revised: 2 August 2022 / Accepted: 6 August 2022 / Published: 10 August 2022
(This article belongs to the Section Bioinformatics and Systems Biology)
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Abstract

There is increasing evidence that many intrinsically disordered regions (IDRs) in proteins play key functional roles through interactions with other proteins or nucleic acids. These interactions often exhibit a context-dependent structural behavior. We hypothesize that low complexity regions (LCRs), often found within IDRs, could have a role in inducing local structure in IDRs. To test this, we predicted IDRs in the human proteome and analyzed their structures or those of homologous sequences in the Protein Data Bank (PDB). We then identified two types of simple LCRs within IDRs: regions with only one (polyX or homorepeats) or with only two types of amino acids (polyXY). We were able to assign structural information from the PDB more often to these LCRs than to the surrounding IDRs (polyX 61.8% > polyXY 50.5% > IDRs 39.7%). The most frequently observed polyX and polyXY within IDRs contained E (Glu) or G (Gly). Structural analyses of these sequences and of homologs indicate that polyEK regions induce helical conformations, while the other most frequent LCRs induce coil structures. Our work proposes bioinformatics methods to help in the study of the structural behavior of IDRs and provides a solid basis suggesting a structuring role of LCRs within them.
Keywords: intrinsically disordered regions; low complexity regions; protein structure; homorepeats intrinsically disordered regions; low complexity regions; protein structure; homorepeats
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MDPI and ACS Style

Gonçalves-Kulik, M.; Mier, P.; Kastano, K.; Cortés, J.; Bernadó, P.; Schmid, F.; Andrade-Navarro, M.A. Low Complexity Induces Structure in Protein Regions Predicted as Intrinsically Disordered. Biomolecules 2022, 12, 1098. https://doi.org/10.3390/biom12081098

AMA Style

Gonçalves-Kulik M, Mier P, Kastano K, Cortés J, Bernadó P, Schmid F, Andrade-Navarro MA. Low Complexity Induces Structure in Protein Regions Predicted as Intrinsically Disordered. Biomolecules. 2022; 12(8):1098. https://doi.org/10.3390/biom12081098

Chicago/Turabian Style

Gonçalves-Kulik, Mariane, Pablo Mier, Kristina Kastano, Juan Cortés, Pau Bernadó, Friederike Schmid, and Miguel A. Andrade-Navarro. 2022. "Low Complexity Induces Structure in Protein Regions Predicted as Intrinsically Disordered" Biomolecules 12, no. 8: 1098. https://doi.org/10.3390/biom12081098

APA Style

Gonçalves-Kulik, M., Mier, P., Kastano, K., Cortés, J., Bernadó, P., Schmid, F., & Andrade-Navarro, M. A. (2022). Low Complexity Induces Structure in Protein Regions Predicted as Intrinsically Disordered. Biomolecules, 12(8), 1098. https://doi.org/10.3390/biom12081098

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