8j7e | pdb_00008j7e

Crystal structure of BRIL in complex with 1b3 Fab

spinqualitylabelsall models 8j7e, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8j7e is a 6 chain structure with sequence from Escherichia coli and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C562_ECOLX Electron-transport protein of unknown function. Publication Abstract from PubMed G-protein-coupled receptors (GPCRs) are a class of integral membrane proteins that detect environmental cues and trigger cellular responses. Deciphering the functional states of GPCRs induced by various ligands has been one of the primary goals in the field. Here we developed an effective universal method for GPCR cryo-electron microscopy structure determination without the need to prepare GPCR-signaling protein complexes. Using this method, we successfully solved the structures of the beta(2)-adrenergic receptor (beta(2)AR) bound to antagonistic and agonistic ligands and the adhesion GPCR ADGRL3 in the apo state. For beta(2)AR, an intermediate state stabilized by the partial agonist was captured. For ADGRL3, the structure revealed that inactive ADGRL3 adopts a compact fold and that large unusual conformational changes on both the extracellular and intracellular sides are required for activation of adhesion GPCRs. We anticipate that this method will open a new avenue for understanding GPCR structure‒function relationships and drug development. A method for structure determination of GPCRs in various states.,Guo Q, He B, Zhong Y, Jiao H, Ren Y, Wang Q, Ge Q, Gao Y, Liu X, Du Y, Hu H, Tao Y Nat Chem Biol. 2024 Jan;20(1):74-82. doi: 10.1038/s41589-023-01389-0. Epub 2023 , Aug 14. PMID:37580554 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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