Creation of artificial protein–protein interactions using α-helices as interfaces

Sota Yagi, Satoshi Akanuma, Akihiko Yamagishi*

*この研究の対応する著者

研究成果: Review article査読

6 被引用数 (Scopus)

抄録

Designing novel protein–protein interactions (PPIs) with high affinity is a challenging task. Directed evolution, a combination of randomization of the gene for the protein of interest and selection using a display technique, is one of the most powerful tools for producing a protein binder. However, the selected proteins often bind to the target protein at an undesired surface. More problematically, some selected proteins bind to their targets even though they are unfolded. Current state-of-the-art computational design methods have successfully created novel protein binders. These computational methods have optimized the non-covalent interactions at interfaces and thus produced artificial protein complexes. However, to date there are only a limited number of successful examples of computationally designed de novo PPIs. De novo design of coiled-coil proteins has been extensively performed and, therefore, a large amount of knowledge of the sequence–structure relationship of coiled-coil proteins has been accumulated. Taking advantage of this knowledge, de novo design of inter-helical interactions has been used to produce artificial PPIs. Here, we review recent progress in the in silico design and rational design of de novo PPIs and the use of α-helices as interfaces.

本文言語English
ページ(範囲)411-420
ページ数10
ジャーナルBiophysical Reviews
10
2
DOI
出版ステータスPublished - 2018 4 1

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 分子生物学

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