Modeling Protein Complexes and Molecular Assemblies Using Computational Methods.
Molecular assembly
PPI
Protein structure prediction
Protein-protein docking, Sequence coevolution
Protein-protein interaction
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
entrez:
13
10
2022
pubmed:
14
10
2022
medline:
18
10
2022
Statut:
ppublish
Résumé
Many biological molecules are assembled into supramolecular complexes that are necessary to perform functions in the cell. Better understanding and characterization of these molecular assemblies are thus essential to further elucidate molecular mechanisms and key protein-protein interactions that could be targeted to modulate the protein binding affinity or develop new binders. Experimental access to structural information on these supramolecular assemblies is often hampered by the size of these systems that make their recombinant production and characterization rather difficult. Computational methods combining both structural data, molecular modeling techniques, and sequence coevolution information can thus offer a good alternative to gain access to the structural organization of protein complexes and assemblies. Herein, we present some computational methods to predict structural models of the protein partners, to search for interacting regions using coevolution information, and to build molecular assemblies. The approach is exemplified using a case study to model the succinate-quinone oxidoreductase heterocomplex.
Identifiants
pubmed: 36227539
doi: 10.1007/978-1-0716-2617-7_4
doi:
Substances chimiques
Proteins
0
Electron Transport Complex II
EC 1.3.5.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
57-77Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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