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3V2Y

Crystal Structure of a Lipid G protein-Coupled Receptor at 2.80A

Summary for 3V2Y
Entry DOI10.2210/pdb3v2y/pdb
Related3v2w
DescriptorSphingosine 1-phosphate receptor 1, Lysozyme chimera (E.C.3.2.1.17), {(3R)-3-amino-4-[(3-hexylphenyl)amino]-4-oxobutyl}phosphonic acid, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordssphingosine, edg receptor, lipid receptor, multiple sclerosis, autoimmunity, structural genomics, psi-biology, gpcr network, gpcr, membrane protein, g protein coupled receptor, membrane, hydrolase
Biological sourceHomo sapiens (Human)
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Total number of polymer chains1
Total formula weight59536.75
Authors
Primary citationHanson, M.A.,Roth, C.B.,Jo, E.,Griffith, M.T.,Scott, F.L.,Reinhart, G.,Desale, H.,Clemons, B.,Cahalan, S.M.,Schuerer, S.C.,Sanna, M.G.,Han, G.W.,Kuhn, P.,Rosen, H.,Stevens, R.C.
Crystal structure of a lipid G protein-coupled receptor.
Science, 335:851-855, 2012
Cited by
PubMed Abstract: The lyso-phospholipid sphingosine 1-phosphate modulates lymphocyte trafficking, endothelial development and integrity, heart rate, and vascular tone and maturation by activating G protein-coupled sphingosine 1-phosphate receptors. Here, we present the crystal structure of the sphingosine 1-phosphate receptor 1 fused to T4-lysozyme (S1P(1)-T4L) in complex with an antagonist sphingolipid mimic. Extracellular access to the binding pocket is occluded by the amino terminus and extracellular loops of the receptor. Access is gained by ligands entering laterally between helices I and VII within the transmembrane region of the receptor. This structure, along with mutagenesis, agonist structure-activity relationship data, and modeling, provides a detailed view of the molecular recognition and requirement for hydrophobic volume that activates S1P(1), resulting in the modulation of immune and stromal cell responses.
PubMed: 22344443
DOI: 10.1126/science.1215904
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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