Control of repeat protein curvature by computational protein design

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...

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Main Authors:	Park, Keunwan, Shen, Betty W., Parmeggiani, Fabio, Huang, Po-Ssu, Stoddard, Barry L., Baker, David
Format:	Online
Language:	English
Published:	2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4318719/

id	pubmed-4318719
recordtype	oai_dc
spelling	pubmed-43187192015-08-01 Control of repeat protein curvature by computational protein design Park, Keunwan Shen, Betty W. Parmeggiani, Fabio Huang, Po-Ssu Stoddard, Barry L. Baker, David Article 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, a set of self-compatible building block modules are designed that when polymerized each 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. 2015-01-12 2015-02 /pmc/articles/PMC4318719/ /pubmed/25580576 http://dx.doi.org/10.1038/nsmb.2938 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Park, Keunwan Shen, Betty W. Parmeggiani, Fabio Huang, Po-Ssu Stoddard, Barry L. Baker, David
spellingShingle	Park, Keunwan Shen, Betty W. Parmeggiani, Fabio Huang, Po-Ssu Stoddard, Barry L. Baker, David Control of repeat protein curvature by computational protein design
author_facet	Park, Keunwan Shen, Betty W. Parmeggiani, Fabio Huang, Po-Ssu Stoddard, Barry L. Baker, David
author_sort	Park, Keunwan
title	Control of repeat protein curvature by computational protein design
title_short	Control of repeat protein curvature by computational protein design
title_full	Control of repeat protein curvature by computational protein design
title_fullStr	Control of repeat protein curvature by computational protein design
title_full_unstemmed	Control of repeat protein curvature by computational protein design
title_sort	control of repeat protein curvature by computational protein design
description	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, a set of self-compatible building block modules are designed that when polymerized each 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.
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4318719/
_version_	1613184762241875968

Control of repeat protein curvature by computational protein design

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