4GBR

N-Terminal T4 Lysozyme Fusion Facilitates Crystallization of a G Protein Coupled Receptor

Summary for 4GBR

• Entry DOI: 10.2210/pdb4gbr/pdb
• Descriptor: Beta-2 adrenergic receptor, Lysozyme, (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol (3 entities in total)
• Functional Keywords: 7 transmembrane helices, g-protein coupled receptor, signal transduction, carazolol, alkylation, membrane, membrane protein-hydrolase complex, membrane protein/hydrolase
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Multi-pass membrane protein: P07550
• Total number of polymer chains: 2
• Total formula weight: 53730.47

Authors

Zou, Y.,Weis, W.I.,Kobilka, B.K. (deposition date: 2012-07-27, release date: 2012-10-24, Last modification date: 2024-10-16)

Primary citation

Zou, Y.,Weis, W.I.,Kobilka, B.K.
N-terminal t4 lysozyme fusion facilitates crystallization of a g protein coupled receptor.
Plos One, 7:e46039-e46039, 2012

PubMed Abstract: A highly crystallizable T4 lysozyme (T4L) was fused to the N-terminus of the β(2) adrenergic receptor (β(2)AR), a G-protein coupled receptor (GPCR) for catecholamines. We demonstrate that the N-terminal fused T4L is sufficiently rigid relative to the receptor to facilitate crystallogenesis without thermostabilizing mutations or the use of a stabilizing antibody, G protein, or protein fused to the 3rd intracellular loop. This approach adds to the protein engineering strategies that enable crystallographic studies of GPCRs alone or in complex with a signaling partner.

PubMed: 23056231
DOI: 10.1371/journal.pone.0046039

Experimental method

X-RAY DIFFRACTION (3.993 Å)