Sequence co-evolution gives 3D contacts and structures of protein complexes.
Elife
; 32014 Sep 25.
Article
em En
| MEDLINE
| ID: mdl-25255213
ABSTRACT
Protein-protein interactions are fundamental to many biological processes. Experimental screens have identified tens of thousands of interactions, and structural biology has provided detailed functional insight for select 3D protein complexes. An alternative rich source of information about protein interactions is the evolutionary sequence record. Building on earlier work, we show that analysis of correlated evolutionary sequence changes across proteins identifies residues that are close in space with sufficient accuracy to determine the three-dimensional structure of the protein complexes. We evaluate prediction performance in blinded tests on 76 complexes of known 3D structure, predict protein-protein contacts in 32 complexes of unknown structure, and demonstrate how evolutionary couplings can be used to distinguish between interacting and non-interacting protein pairs in a large complex. With the current growth of sequences, we expect that the method can be generalized to genome-wide elucidation of protein-protein interaction networks and used for interaction predictions at residue resolution.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Genoma Bacteriano
/
Proteínas de Escherichia coli
/
Mapeamento de Interação de Proteínas
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Escherichia coli
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Elife
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Estados Unidos