Control of repeat-protein curvature by computational protein design

Park, K., Shen, B. W., Parmeggiani, F. ORCID: https://orcid.org/0000-0001-8548-1090, Huang, P. S., Stoddard, B. and Baker, D. 2015. Control of repeat-protein curvature by computational protein design. Nature Structural and Molecular Biology 22 (2) , pp. 167-174. 10.1038/nsmb.2938

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Abstract

Shape complementarity is an important component of molecular recognition, and the ability to precisely adjust the shape of a binding scaffold to match a target of interest would greatly facilitate the creation of high-affinity protein reagents and therapeutics. Here we describe a general approach to control the shape of the binding surface on repeat-protein scaffolds and apply it to leucine-rich-repeat proteins. First, self-compatible building-block modules are designed that, when polymerized, generate surfaces with unique but constant curvatures. Second, a set of junction modules that connect the different building blocks are designed. Finally, new proteins with custom-designed shapes are generated by appropriately combining building-block and junction modules. Crystal structures of the designs illustrate the power of the approach in controlling repeat-protein curvature.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Pharmacy
Publisher:	Nature Publishing Group
ISSN:	1545-9993
Last Modified:	18 Oct 2024 09:40
URI:	https://orca.cardiff.ac.uk/id/eprint/172218

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