5HZK

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

Summary for 5HZK

• Entry DOI: 10.2210/pdb5hzk/pdb
• Descriptor: Cell division control protein 42 homolog, Intersectin-1,NPH1-1,Intersectin-1, GUANOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: signaling protein, photoswitch, chimera, complex
• Biological source: Homo sapiens (Human); More
• Cellular location: Cell membrane ; Lipid-anchor ; Cytoplasmic side : P60953; Endomembrane system : Q15811
• Total number of polymer chains: 4
• Total formula weight: 160527.68

Authors

Tarnawski, M.,Dagliyan, O.,Chu, P.H.,Shirvanyants, D.,Dokholyan, N.V.,Hahn, K.M.,Schlichting, I. (deposition date: 2016-02-02, release date: 2016-12-21, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.3 Å)