5HZK

Crystal structure of photoinhibitable Intersectin1 containing wildtype LOV2 domain in complex with Cdc42

5HZK の概要

• エントリーDOI: 10.2210/pdb5hzk/pdb
• 分子名称: Cell division control protein 42 homolog, Intersectin-1,NPH1-1,Intersectin-1, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: signaling protein, photoswitch, chimera, complex
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cell membrane ; Lipid-anchor ; Cytoplasmic side : P60953; Endomembrane system : Q15811
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 160527.68

構造登録者

Tarnawski, M.,Dagliyan, O.,Chu, P.H.,Shirvanyants, D.,Dokholyan, N.V.,Hahn, K.M.,Schlichting, I. (登録日: 2016-02-02, 公開日: 2016-12-21, 最終更新日: 2024-01-10)

主引用文献

Dagliyan, O.,Tarnawski, M.,Chu, P.H.,Shirvanyants, D.,Schlichting, I.,Dokholyan, N.V.,Hahn, K.M.
Engineering extrinsic disorder to control protein activity in living cells.
Science, 354:1441-1444, 2016

PubMed Abstract: Optogenetic and chemogenetic control of proteins has revealed otherwise inaccessible facets of signaling dynamics. Here, we use light- or ligand-sensitive domains to modulate the structural disorder of diverse proteins, thereby generating robust allosteric switches. Sensory domains were inserted into nonconserved, surface-exposed loops that were tight and identified computationally as allosterically coupled to active sites. Allosteric switches introduced into motility signaling proteins (kinases, guanosine triphosphatases, and guanine exchange factors) controlled conversion between conformations closely resembling natural active and inactive states, as well as modulated the morphodynamics of living cells. Our results illustrate a broadly applicable approach to design physiological protein switches.

PubMed: 27980211
DOI: 10.1126/science.aah3404

実験手法

X-RAY DIFFRACTION (3.3 Å)