Motif-driven design of protein–protein interfaces

Daniel Adriano Silva, Bruno E. Correia, Erik Procko

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Protein–protein interfaces regulate many critical processes for cellular function. The ability to accurately control and regulate these molecular interactions is of major interest for biomedical and synthetic biology applications, as well as to address fundamental biological questions. In recent years, computational protein design has emerged as a tool for designing novel protein–protein interactions with functional relevance. Although attractive, these computational tools carry a steep learning curve. In order to make some of these methods more accessible, we present detailed descriptions and examples of ROSETTA computational protocols for the design of functional protein binders using seeded protein interface design. In these protocols, a motif of known structure that interacts with the target site is grafted into a scaffold protein, followed by design of the surrounding interaction surface.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages285-304
Number of pages20
DOIs
StatePublished - May 1 2016

Publication series

NameMethods in Molecular Biology
Volume1414
ISSN (Print)1064-3745

Keywords

  • Computational protein design
  • Interface design
  • Motif grafting
  • Protein–protein interaction
  • ROSETTA

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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    Silva, D. A., Correia, B. E., & Procko, E. (2016). Motif-driven design of protein–protein interfaces. In Methods in Molecular Biology (pp. 285-304). (Methods in Molecular Biology; Vol. 1414). Humana Press Inc.. https://doi.org/10.1007/978-1-4939-3569-7_17