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Structure paper

TitleUnsaturated bond recognition leads to biased signal in a fatty acid receptor.
Journal, issue, pagesScience, Vol. 380, Issue 6640, Page eadd6220, Year 2023
Publish dateApr 7, 2023
AuthorsChunyou Mao / Peng Xiao / Xiao-Na Tao / Jiao Qin / Qing-Tao He / Chao Zhang / Sheng-Chao Guo / Ya-Qin Du / Li-Nan Chen / Dan-Dan Shen / Zhi-Shuai Yang / Han-Qiong Zhang / Shen-Ming Huang / Yong-Hao He / Jie Cheng / Ya-Ni Zhong / Pan Shang / Jun Chen / Dao-Lai Zhang / Qian-Lang Wang / Mei-Xia Liu / Guo-Yu Li / Yongyuan Guo / H Eric Xu / Chuanxin Wang / Cheng Zhang / Shiqing Feng / Xiao Yu / Yan Zhang / Jin-Peng Sun /
PubMed AbstractIndividual free fatty acids (FAs) play important roles in metabolic homeostasis, many through engagement with more than 40G protein-coupled receptors. Searching for receptors to sense beneficial ...Individual free fatty acids (FAs) play important roles in metabolic homeostasis, many through engagement with more than 40G protein-coupled receptors. Searching for receptors to sense beneficial omega-3 FAs of fish oil enabled the identification of GPR120, which is involved in a spectrum of metabolic diseases. Here, we report six cryo-electron microscopy structures of GPR120 in complex with FA hormones or TUG891 and G or G trimers. Aromatic residues inside the GPR120 ligand pocket were responsible for recognizing different double-bond positions of these FAs and connect ligand recognition to distinct effector coupling. We also investigated synthetic ligand selectivity and the structural basis of missense single-nucleotide polymorphisms. We reveal how GPR120 differentiates rigid double bonds and flexible single bonds. The knowledge gleaned here may facilitate rational drug design targeting to GPR120.
External linksScience / PubMed:36862765
MethodsEM (single particle)
Resolution2.52 - 3.1 Å
Structure data

29736

8g59

EMDB-29736, PDB-8g59:
Cryo-EM structure of the TUG891 bound GPR120-Giq complex
Method: EM (single particle) / Resolution: 2.64 Å

35356

8id3

EMDB-35356, PDB-8id3:
Cryo-EM structure of the 9-hydroxystearic acid bound GPR120-Gi complex
Method: EM (single particle) / Resolution: 3.1 Å

35357

8id4

EMDB-35357, PDB-8id4:
Cryo-EM structure of the linoleic acid bound GPR120-Gi complex
Method: EM (single particle) / Resolution: 3.1 Å

35358

8id6

EMDB-35358, PDB-8id6:
Cryo-EM structure of the oleic acid bound GPR120-Gi complex
Method: EM (single particle) / Resolution: 2.8 Å

35359

8id8

EMDB-35359, PDB-8id8:
Cryo-EM structure of the TUG891 bound GPR120-Gi complex
Method: EM (single particle) / Resolution: 3.0 Å

35360

8id9

EMDB-35360, PDB-8id9:
Cryo-EM structure of the eicosapentaenoic acid bound GPR120-Gi complex
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-35522: Cryo-EM structure of the TUG891 bound GPR120-Giq complex(mask on receptor)
Method: EM (single particle) / Resolution: 2.89 Å

EMDB-35523: Cryo-EM structure of the TUG891 bound GPR120-Giq complex(mask on Giq-scFV16 complex)
Method: EM (single particle) / Resolution: 2.52 Å

EMDB-35524: Cryo-EM structure of the eicosapentaenoic acid bound GPR120-Gi1 complex(mask on receptor)
Method: EM (single particle) / Resolution: 2.91 Å

EMDB-35525: Cryo-EM structure of the eicosapentaenoic acid bound GPR120-Gi1 complex(mask on Gil-scFV16 complex)
Method: EM (single particle) / Resolution: 2.71 Å

EMDB-35529: Cryo-EM structure of the TUG891 bound GPR120-Giq complex (consensus map)
Method: EM (single particle) / Resolution: 2.64 Å

EMDB-35533: Cryo-EM structure of the eicosapentaenoic acid bound GPR120-Gi complex(consensus map)
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-YN9:
3-{4-[(4-fluoro-4'-methyl[1,1'-biphenyl]-2-yl)methoxy]phenyl}propanoic acid

ChemComp-7NR:
9-Hydroxyoctadecanoic acid

ChemComp-EIC:
LINOLEIC ACID / Linoleic acid

ChemComp-HOH:
WATER / Water

ChemComp-OLA:
OLEIC ACID / Oleic acid

ChemComp-EPA:
5,8,11,14,17-EICOSAPENTAENOIC ACID / medication*YM / Ethyl eicosapentaenoic acid

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / GPCR / GPR120 / complex / fatty acid hormones

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