4R5C

Crystal structure of computational designed leucine rich repeats DLRR_E in space group of P212121

Summary for 4R5C

• Entry DOI: 10.2210/pdb4r5c/pdb
• Related: 4R58 4R5D 4R6F 4R6G 4R6J
• Descriptor: Leucine rich repeat protein, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: leucine rich repeat (lrr) protein, de novo protein
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 33363.29

Authors

Shen, B.W.,Stoddard, B.L. (deposition date: 2014-08-21, release date: 2015-01-07, Last modification date: 2024-02-28)

Primary citation

Park, K.,Shen, B.W.,Parmeggiani, F.,Huang, P.S.,Stoddard, B.L.,Baker, D.
Control of repeat-protein curvature by computational protein design.
Nat.Struct.Mol.Biol., 22:167-174, 2015

PubMed 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.

PubMed: 25580576
DOI: 10.1038/nsmb.2938

Experimental method

X-RAY DIFFRACTION (1.93 Å)