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7M8W

XFEL crystal structure of the prostaglandin D2 receptor CRTH2 in complex with 15R-methyl-PGD2

Summary for 7M8W
Entry DOI10.2210/pdb7m8w/pdb
DescriptorProstaglandin D2 receptor 2, Endolysin chimera, 15R-methyl-prostaglandin D2, SODIUM ION, ... (6 entities in total)
Functional Keywordsprostaglandin d2 receptor, crth2, 15r-methyl-pgd2, g protein-coupled receptor, gpcr, endolysin fusion, membrane protein, lcp
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains1
Total formula weight53287.62
Authors
Shiriaeva, A.,Han, G.W.,Cherezov, V. (deposition date: 2021-03-30, release date: 2021-08-25, Last modification date: 2023-10-18)
Primary citationLiu, H.,Deepak, R.N.V.K.,Shiriaeva, A.,Gati, C.,Batyuk, A.,Hu, H.,Weierstall, U.,Liu, W.,Wang, L.,Cherezov, V.,Fan, H.,Zhang, C.
Molecular basis for lipid recognition by the prostaglandin D 2 receptor CRTH2.
Proc.Natl.Acad.Sci.USA, 118:-, 2021
Cited by
PubMed Abstract: Prostaglandin D (PGD) signals through the G protein-coupled receptor (GPCR) CRTH2 to mediate various inflammatory responses. CRTH2 is the only member of the prostanoid receptor family that is phylogenetically distant from others, implying a nonconserved mechanism of lipid action on CRTH2. Here, we report a crystal structure of human CRTH2 bound to a PGD derivative, 15R-methyl-PGD (15mPGD), by serial femtosecond crystallography. The structure revealed a "polar group in"-binding mode of 15mPGD contrasting the "polar group out"-binding mode of PGE in its receptor EP3. Structural comparison analysis suggested that these two lipid-binding modes, associated with distinct charge distributions of ligand-binding pockets, may apply to other lipid GPCRs. Molecular dynamics simulations together with mutagenesis studies also identified charged residues at the ligand entry port that function to capture lipid ligands of CRTH2 from the lipid bilayer. Together, our studies suggest critical roles of charge environment in lipid recognition by GPCRs.
PubMed: 34341104
DOI: 10.1073/pnas.2102813118
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.61 Å)
Structure validation

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