4R58: Crystal Structure Of Computational Designed Leucine Rich Repeats Dlrr_a In Space Group P21

Citation:
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.
PDB ID: 4R58Download
MMDB ID: 126063
PDB Deposition Date: 2014/8/20
Updated in MMDB: 2015/02
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 4R58: monomeric; determined by author and by software (PISA)
Molecular Components in 4R58
Label Count Molecule
Protein (1 molecule)
1
Leucine Rich Repeat Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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