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TitleStructural basis for lysophosphatidic acid recognition and atypical Gα coupling by LPAR5.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 123, Issue 25, Page e2537482123, Year 2026
Publish dateJun 23, 2026
AuthorsXin Li / Kai Wang / Zhongliang Xing / Min Zhang / Wen Hu / Qingning Yuan / H Eric Xu / Li-Hua Zhao /
PubMed AbstractLysophosphatidic acid receptor 5 (LPAR5) is a non-endothelial differentiation gene class A G protein-coupled receptor that regulates neuropathic pain, itch, and cancer progression through coupling to ...Lysophosphatidic acid receptor 5 (LPAR5) is a non-endothelial differentiation gene class A G protein-coupled receptor that regulates neuropathic pain, itch, and cancer progression through coupling to G proteins. Here, we report the cryo-EM structure of LPAR5 bound to 1-oleoyl-lysophosphatidic acid (LPA) in complex with G at 2.96 Å resolution, revealing a distinct mode of receptor activation and G protein coupling. The phosphate headgroup of LPA forms extensive polar interactions with residues from extracellular loop 2 and transmembrane helices TM5-TM7, while the lipid tail inserts into a deep hydrophobic cavity formed by TM3-TM5. Site-directed mutagenesis confirms the functional importance of these interactions. Remarkably, LPAR5 exhibits a noncanonical G protein coupling mode. Unlike previously reported GPCR-G protein structures in which the Gα C-terminal α5 helix ("wavy hook") primarily engages TM6, the wavy hook in LPAR5 is positioned toward the intracellular loop 1-helix 8 interface. This configuration is associated with limited TM6 outward displacement and modest rearrangement at the toggle-switch position (6.48). The resulting interface is stabilized by receptor-specific interactions and supported by functional data. Together, these findings reveal an alternative mode of GPCR-G protein coupling and highlight the structural plasticity underlying signaling specificity in LPA receptors.
External linksProc Natl Acad Sci U S A / PubMed:42313925 / PubMed Central
MethodsEM (single particle)
Resolution2.96 Å
Structure data

67439

20zx

EMDB-67439, PDB-20zx:
Cryo-EM structure of Gq-coupled LPAR5 in complex with LPA
Method: EM (single particle) / Resolution: 2.96 Å

Chemicals

ChemComp-UBL:
[(2R)-2-oxidanyl-3-phosphonooxy-propyl] (Z)-octadec-9-enoate

Source
  • homo sapiens (human)
  • rattus norvegicus (Norway rat)
  • bos taurus (domestic cattle)
KeywordsMEMBRANE PROTEIN / LPAR5 / LPA

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