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TitleIdentification, structure, and agonist design of an androgen membrane receptor.
Journal, issue, pagesCell, Vol. 188, Issue 6, Page 1589-1604.e24, Year 2025
Publish dateMar 20, 2025
AuthorsZhao Yang / Yu-Qi Ping / Ming-Wei Wang / Chao Zhang / Shu-Hua Zhou / Yue-Tong Xi / Kong-Kai Zhu / Wei Ding / Qi-Yue Zhang / Zhi-Chen Song / Ru-Jia Zhao / Zi-Lu He / Meng-Xin Wang / Lei Qi / Christian Ullmann / Albert Ricken / Torsten Schöneberg / Zhen-Ji Gan / Xiao Yu / Peng Xiao / Fan Yi / Ines Liebscher / Jin-Peng Sun /
PubMed AbstractAndrogens, such as 5α-dihydrotestosterone (5α-DHT), regulate numerous functions by binding to nuclear androgen receptors (ARs) and potential unknown membrane receptors. Here, we report that the ...Androgens, such as 5α-dihydrotestosterone (5α-DHT), regulate numerous functions by binding to nuclear androgen receptors (ARs) and potential unknown membrane receptors. Here, we report that the androgen 5α-DHT activates membrane receptor GPR133 in muscle cells, thereby increasing intracellular cyclic AMP (cAMP) levels and enhancing muscle strength. Further cryoelectron microscopy (cryo-EM) structural analysis of GPR133-Gs in complex with 5α-DHT or its derivative methenolone (MET) reveals the structural basis for androgen recognition. Notably, the presence of the "Φ(F/L)-F-W" and the "F××N/D" motifs, which recognize the hydrophobic steroid core and polar groups, respectively, are common in adhesion GPCRs (aGPCRs), suggesting that many aGPCRs may recognize different steroid hormones. Finally, we exploited in silico screening methods to identify a small molecule, AP503, which activates GPR133 and separates the beneficial muscle-strengthening effects from side effects mediated by AR. Thus, GPR133 represents an androgen membrane receptor that contributes to normal androgen physiology and has important therapeutic potentials.
External linksCell / PubMed:39884271
MethodsEM (single particle)
Resolution2.75 - 3.53 Å
Structure data

38183

8x9s

EMDB-38183, PDB-8x9s:
Identification, structure and agonist design of an androgen membrane receptor.
Method: EM (single particle) / Resolution: 3.49 Å

38184

8x9t

EMDB-38184, PDB-8x9t:
Identification, structure and agonist design of an androgen membrane receptor
Method: EM (single particle) / Resolution: 2.75 Å

38185

8x9u

EMDB-38185, PDB-8x9u:
Identification, structure and agonist design of an androgen membrane receptor
Method: EM (single particle) / Resolution: 2.88 Å

60917

9iv1

EMDB-60917, PDB-9iv1:
Identification, structure and agonist design of an androgen membrane receptor.
Method: EM (single particle) / Resolution: 2.98 Å

60918

9iv2

EMDB-60918, PDB-9iv2:
Identification, structure and agonist design of an androgen membrane receptor.
Method: EM (single particle) / Resolution: 3.53 Å

Chemicals

ChemComp-DHT:
5-ALPHA-DIHYDROTESTOSTERONE / hormone*YM


ChemComp, No image

ChemComp-YNH:
Unknown entry

PDB-1lu1:
THE STRUCTURE OF THE DOLICHOS BIFLORUS SEED LECTIN IN COMPLEX WITH THE FORSSMAN DISACCHARIDE

Source
  • bos taurus (domestic cattle)
  • rattus norvegicus (Norway rat)
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / Complex / agonist / GPCR / adhesion GPCR / GPR133 / GPCR-G protein complex

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