Sequence and Structure Properties Uncover the Natural Classification of Protein Complexes Formed by Intrinsically Disordered Proteins via Mutual Synergistic Folding.

Mészáros, Bálint; Dobson, László; Fichó, Erzsébet; Simon, István

Mészáros, Bálint; Dobson, László; Fichó, Erzsébet; Simon, István.

Afiliación

Mészáros B; MTA-ELTE Momentum Bioinformatics Research Group, Department of Biochemistry, Eötvös Loránd University, Pázmány Péter stny 1/c, H-1117 Budapest, Hungary. bmeszaros@caesar.elte.hu.
Dobson L; European Molecular Biology Laboratory, Structural and Computational Biology Unit, Meyerhofstraße 1, 69117 Heidelberg, Germany. bmeszaros@caesar.elte.hu.
Fichó E; Protein Structure Research Group, Institute of Enzymology, RCNS, HAS, Magyar Tudósok krt 2, H-1117 Budapest, Hungary. bmeszaros@caesar.elte.hu.
Simon I; Membrane Protein Bioinformatics Research Group, Institute of Enzymology, RCNS, HAS, Magyar Tudósok krt 2, H-1117 Budapest, Hungary. dobson.laszlo.imre@itk.ppke.hu.

Int J Mol Sci ; 20(21)2019 Nov 01.

Article en En | MEDLINE | ID: mdl-31683980

RESUMEN

Intrinsically disordered proteins mediate crucial biological functions through their interactions with other proteins. Mutual synergistic folding (MSF) occurs when all interacting proteins are disordered, folding into a stable structure in the course of the complex formation. In these cases, the folding and binding processes occur in parallel, lending the resulting structures uniquely heterogeneous features. Currently there are no dedicated classification approaches that take into account the particular biological and biophysical properties of MSF complexes. Here, we present a scalable clustering-based classification scheme, built on redundancy-filtered features that describe the sequence and structure properties of the complexes and the role of the interaction, which is directly responsible for structure formation. Using this approach, we define six major types of MSF complexes, corresponding to biologically meaningful groups. Hence, the presented method also shows that differences in binding strength, subcellular localization, and regulation are encoded in the sequence and structural properties of proteins. While current protein structure classification methods can also handle complex structures, we show that the developed scheme is fundamentally different, and since it takes into account defining features of MSF complexes, it serves as a better representation of structures arising through this specific interaction mode.

Asunto(s)

Proteínas Intrínsecamente Desordenadas/química; Pliegue de Proteína; Estructura Secundaria de Proteína; Estructura Terciaria de Proteína; Secuencia de Aminoácidos; Animales; Análisis por Conglomerados; Humanos; Proteínas Intrínsecamente Desordenadas/clasificación; Proteínas Intrínsecamente Desordenadas/metabolismo; Cinética; Modelos Moleculares; Unión Proteica; Termodinámica

Palabras clave

IDP; coupled folding and binding; fold recognition; intrinsically disordered protein; mutual synergistic folding; proteinprotein interaction; structural analysis; structure-based classification

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Estructura Terciaria de Proteína / Estructura Secundaria de Proteína / Pliegue de Proteína / Proteínas Intrínsecamente Desordenadas Límite: Animals / Humans Idioma: En Revista: Int J Mol Sci Año: 2019 Tipo del documento: Article País de afiliación: Hungria Pais de publicación: Suiza

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