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8RQQ

In meso structure of the adenosine A2a G protein-coupled receptor, A2aR, in 7.10 monoacylglycerol

This is a non-PDB format compatible entry.
Summary for 8RQQ
Entry DOI10.2210/pdb8rqq/pdb
DescriptorAdenosine receptor A2a,Soluble cytochrome b562, 4-{2-[(7-amino-2-furan-2-yl[1,2,4]triazolo[1,5-a][1,3,5]triazin-5-yl)amino]ethyl}phenol, CHOLESTEROL, ... (8 entities in total)
Functional Keywordsg protein-coupled receptor, membrane protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains1
Total formula weight54761.37
Authors
Smithers, L.,Krawinski, P.,Caffrey, M. (deposition date: 2024-01-19, release date: 2024-04-03, Last modification date: 2024-11-20)
Primary citationKrawinski, P.,Smithers, L.,van Dalsen, L.,Boland, C.,Ostrovitsa, N.,Perez, J.,Caffrey, M.
7.10 MAG. A Novel Host Monoacylglyceride for In Meso (Lipid Cubic Phase) Crystallization of Membrane Proteins.
Cryst.Growth Des., 24:2985-3001, 2024
Cited by
PubMed Abstract: A novel monoacylglycerol, 7.10 MAG, has been produced for use in the (lipid cubic phase) crystallization of membrane proteins and complexes. 7.10 MAG differs from monoolein, the most extensively used lipid for crystallization, in that it is shorter in chain length by one methylene and its cis olefinic bond is two carbons closer to the glycerol headgroup. These changes in structure alter the phase behavior of the hydrated lipid and the microstructure of the corresponding mesophases formed. Temperature-composition phase diagrams for 7.10 MAG have been constructed using small- and wide-angle X-ray scattering over a range of temperatures and hydration levels that span those used for crystallization. The phase diagrams include lamellar crystalline, fluid isotropic, lamellar liquid-crystalline, cubic-3 and cubic-3 phases, as observed with monoolein. Conspicuous by its absence is the inverted hexagonal phase which is rationalized on the basis of 7.10 MAG's chemical constitution. The cubic phase prepared with the new lipid facilitates the growth of crystals that were used to generate high-resolution structures of intramembrane β-barrel and α-helical proteins. Compatibility of fully hydrated 7.10 MAG with cholesterol and phosphatidylcholine means that these two lipids can be used as additives to optimize crystallogenesis in screening trials with 7.10 MAG as the host lipid.
PubMed: 38585376
DOI: 10.1021/acs.cgd.4c00087
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.37 Å)
Structure validation

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PDB entries from 2024-11-20

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