4gbr | pdb_00004gbr

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

spinqualitylabelsall models 4gbr, resolution 3.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4gbr is a 2 chain structure with sequence from Enterobacteria phage t4 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CAU Gene: ADRB2, ADRB2R, B2AR (Homo sapiens), E (Enterobacteria phage T4) Activity: Lysozyme, with EC number 3.2.1.17 Resources: FirstGlance, OCA, RCSB, PDBsum Function [ADRB2_HUMAN] Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. [LYS_BPT4] Helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan. Publication Abstract from PubMed A highly crystallizable T4 lysozyme (T4L) was fused to the N-terminus of the beta(2) adrenergic receptor (beta(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. N-terminal t4 lysozyme fusion facilitates crystallization of a g protein coupled receptor.,Zou Y, Weis WI, Kobilka BK PLoS One. 2012;7(10):e46039. doi: 10.1371/journal.pone.0046039. Epub 2012 Oct 4. PMID:23056231 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Adrenergic receptor Lysozyme 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA