PDBsum entry 4r5c

De novo protein

PDB id: 4r5c

Contents

Protein chain

304 a.a.

Ligands

EDO ×2

Waters ×112

PDB id:

4r5c

Name:

De novo protein

Title:

Crystal structure of computational designed leucine rich repeats dlrr_e in space group of p212121

Structure:

Leucine rich repeat protein. Chain: a. Engineered: yes

Source:

Synthetic construct. Organism_taxid: 32630. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.93Å R-factor: 0.160 R-free: 0.222

Authors:

B.W.Shen,B.L.Stoddard

Key ref:

K.Park et al. (2015). Control of repeat-protein curvature by computational protein design. Nat Struct Biol, 22, 167-174. PubMed id: 25580576 DOI: 10.1038/nsmb.2938

Date:

21-Aug-14 Release date: 07-Jan-15

Protein chain

No UniProt id for this chain

Struc: 304 a.a.

DOI no: 10.1038/nsmb.2938

Nat Struct Biol 22:167-174 (2015)

PubMed id: 25580576

Control of repeat-protein curvature by computational protein design.

K.Park, B.W.Shen, F.Parmeggiani, P.S.Huang, B.L.Stoddard, D.Baker.

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.