Artikel ; Online: ZEPPI: Proteome-scale sequence-based evaluation of protein-protein interaction models.
Proceedings of the National Academy of Sciences of the United States of America
2024 Band 121, Heft 21, Seite(n) e2400260121
Abstract: We introduce ZEPPI (Z-score Evaluation of Protein-Protein Interfaces), a framework to evaluate structural models of a complex based on sequence coevolution and conservation involving residues in protein-protein interfaces. The ZEPPI score is calculated ... ...
Abstract | We introduce ZEPPI (Z-score Evaluation of Protein-Protein Interfaces), a framework to evaluate structural models of a complex based on sequence coevolution and conservation involving residues in protein-protein interfaces. The ZEPPI score is calculated by comparing metrics for an interface to those obtained from randomly chosen residues. Since contacting residues are defined by the structural model, this obviates the need to account for indirect interactions. Further, although ZEPPI relies on species-paired multiple sequence alignments, its focus on interfacial residues allows it to leverage quite shallow alignments. ZEPPI can be implemented on a proteome-wide scale and is applied here to millions of structural models of dimeric complexes in the |
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Mesh-Begriff(e) | Proteome/metabolism ; Humans ; Protein Interaction Mapping/methods ; Models, Molecular ; Escherichia coli/metabolism ; Escherichia coli/genetics ; Databases, Protein ; Protein Binding ; Escherichia coli Proteins/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/genetics ; Proteins/chemistry ; Proteins/metabolism ; Sequence Alignment |
Sprache | Englisch |
Erscheinungsdatum | 2024-05-14 |
Erscheinungsland | United States |
Dokumenttyp | Journal Article |
ZDB-ID | 209104-5 |
ISSN | 1091-6490 ; 0027-8424 |
ISSN (online) | 1091-6490 |
ISSN | 0027-8424 |
DOI | 10.1073/pnas.2400260121 |
Datenquelle | MEDical Literature Analysis and Retrieval System OnLINE |
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