4R5D

Crystal structure of computational designed leucine rich repeats DLRR_G3 in space group F222

4R5D の概要

• エントリーDOI: 10.2210/pdb4r5d/pdb
• 関連するPDBエントリー: 4R58 4R5C 4R6F 4R6G 4R6J
• 分子名称: Leucine rich repeat protein, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: leucine rich repeat (lrr) protein, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48551.15

構造登録者

Shen, B.W.,Stoddard, B.L. (登録日: 2014-08-21, 公開日: 2015-01-07, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.53 Å)