Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-10241
Authors: Gonçalves-Kulik, Mariane
Mier, Pablo
Kastano, Kristina
Cortés, Juan
Bernadó, Pau
Schmid, Friederike
Andrade-Navarro, Miguel A.
Title: Low complexity induces structure in protein regions predicted as intrinsically disordered
Online publication date: 26-Mar-2024
Year of first publication: 2022
Language: english
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
DDC: 570 Biowissenschaften
570 Life sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 10 Biologie
Place: Mainz
ROR: https://ror.org/023b0x485
DOI: http://doi.org/10.25358/openscience-10241
Version: Published version
Publication type: Zeitschriftenaufsatz
Document type specification: Scientific article
License: CC BY
Information on rights of use: https://creativecommons.org/licenses/by/4.0/
Journal: Biomolecules
12
8
Pages or article number: 1098
Publisher: MDPI
Publisher place: Basel
Issue date: 2022
ISSN: 2218-273X
Publisher DOI: 10.3390/biom12081098
Appears in collections:DFG-491381577-G

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