4.5 Article

Repeat proteins: designing new shapes and functions for solenoid folds

Journal

CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 68, Issue -, Pages 208-214

Publisher

CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2021.02.002

Keywords

-

Funding

  1. School of Chemistry, University of Bristol through the EPSRC Doctoral Training Partnership
  2. EPSRC Early Career fellowship [EP/S017542/1]

Ask authors/readers for more resources

The modular nature of repeat proteins has led to the design of novel sequences and structures with a broad set of design approaches. These proteins have found applications in molecular recognition by taking advantage of their natural ability to bind proteins, peptides and nucleic acids. New architectures combining different types of repeat can be easily scalable by changing the number of repeats and quickly generated using existing modular building blocks.
The modular nature of repeat proteins has inspired the design of regular and completely novel sequences and structures. Research in the past years has provided a broad set of design approaches and new repeat proteins that have found applications in molecular recognition, taking advantage of the natural ability of some of these families to bind proteins, peptides and nucleic acids. Here, we provide an overview on the recent trends in design of repeat proteins, particularly solenoid folds, and their applications. By exploiting the intrinsic modularity of repeats, new architectures have been designed that combine different types of repeat, are easily scalable by changing the number of repeats and can be quickly generated by using existing modular building blocks.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available