3V2Y
Crystal Structure of a Lipid G protein-Coupled Receptor at 2.80A
Summary for 3V2Y
Entry DOI | 10.2210/pdb3v2y/pdb |
Related | 3v2w |
Descriptor | Sphingosine 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 Keywords | sphingosine, edg receptor, lipid receptor, multiple sclerosis, autoimmunity, structural genomics, psi-biology, gpcr network, gpcr, membrane protein, g protein coupled receptor, membrane, hydrolase |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 1 |
Total formula weight | 59536.75 |
Authors | Hanson, 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.,GPCR Network (GPCR) (deposition date: 2011-12-12, release date: 2012-02-15, Last modification date: 2024-11-27) |
Primary citation | Hanson, 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: 22344443DOI: 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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