The Crystal Structure of Sphingosine

2132 WordsFeb 26, 20188 Pages
In the PDBID 3V2Y, the crystal structure of the sphingosine-1-phosphate receptor subtype 1 is fused to T4-lysozyme. Fusion of the third intracellular loop to the T4-lysozyme rendered soluble crystal junctions (Rosen H et al, 2013) for the rapidly disintegrating microcrystals (Hanson MA et al, 2012). Structure elements of S1PR1 The structural observations gained from antagonist-preserved structures of Rhodopsin-like GPCRs show that the typical orientation of the seven transmembrane domains have significant overlap. The minute overlap is produced depending on the helix bundle, tilt and the specific interactions (hydrophobic and electrostatic). This specific overlap is important for co-ordinated signaling by the different GPCRs (Rosen H et al, 2013). GPCRs possess an extracellular domain consisting of the N terminus and three extracellular loops. However, a number of prominent features are associated with the Ligand Binding Pocket in the S1P1 receptor. The extracellular region of S1PR1 is significantly ordered. This is due to the N terminus comprising a well-ordered α-helix that projects the top of the receptor. This contributes to binding interactions and forms a helix-cap, which occludes access to the amphipathic binding pocket (Hanson MA et al, 2012). The three loops, namely, ECL1 amidst helices II and III, ECL2 formed between helices IV and V and ECL3 in helices VI and VII, also make up the extracellular region. Both ECL1 and ECL2 are tightly packed against the

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