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TitleMolecular Determinant Underlying Selective Coupling of Primary G-Protein by Class A GPCRs.
Journal, issue, pagesAdv Sci (Weinh), Vol. 11, Issue 23, Page e2310120, Year 2024
Publish dateApr 22, 2024
AuthorsQingya Shen / Xinyan Tang / Xin Wen / Shizhuo Cheng / Peng Xiao / Shao-Kun Zang / Dan-Dan Shen / Lei Jiang / Yanrong Zheng / Huibing Zhang / Haomang Xu / Chunyou Mao / Min Zhang / Weiwei Hu / Jin-Peng Sun / Yan Zhang / Zhong Chen /
PubMed AbstractG-protein-coupled receptors (GPCRs) transmit downstream signals predominantly via G-protein pathways. However, the conformational basis of selective coupling of primary G-protein remains elusive. ...G-protein-coupled receptors (GPCRs) transmit downstream signals predominantly via G-protein pathways. However, the conformational basis of selective coupling of primary G-protein remains elusive. Histamine receptors HR and HR couple with G- or G-proteins respectively. Here, three cryo-EM structures of HR-G and HR-G complexes are presented at a global resolution of 2.6-2.7 Å. These structures reveal the unique binding pose for endogenous histamine in HR, wherein the amino group interacts with E206 of HR instead of the conserved D114 of other aminergic receptors. Furthermore, comparative analysis of the HR-G and HR-G complexes reveals that the structural geometry of TM5/TM6 determines the primary G-protein selectivity in histamine receptors. Machine learning (ML)-based structuromic profiling and functional analysis of class A GPCR-G-protein complexes illustrate that TM5 length, TM5 tilt, and TM6 outward movement are key determinants of the G and G selectivity among the whole Class A family. Collectively, the findings uncover the common structural geometry within class A GPCRs that determines the primary G- and G-coupling selectivity.
External linksAdv Sci (Weinh) / PubMed:38647423 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.0 Å
Structure data

39582

8yut

EMDB-39582, PDB-8yut:
Cryo-EM structure of the amthamine-bound H2R-Gs complex
Method: EM (single particle) / Resolution: 2.7 Å

39583

8yuu

EMDB-39583, PDB-8yuu:
Cryo-EM structure of the histamine-bound H3R-Gi complex
Method: EM (single particle) / Resolution: 2.7 Å

39584

8yuv

EMDB-39584, PDB-8yuv:
Cryo-EM structure of the immepip-bound H3R-Gi complex
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

PDB-1d67:
THE MOLECULAR STRUCTURE OF AN IDARUBICIN-D(TGATCA) COMPLEX AT HIGH RESOLUTION

ChemComp-CLR:
CHOLESTEROL

ChemComp-HSM:
HISTAMINE / neurotransmitter, hormone*YM

PDB-1ly4:
Analysis of quinazoline and PYRIDO[2,3D]PYRIMIDINE N9-C10 reversed bridge antifolates in complex with NADP+ and Pneumocystis carinii dihydrofolate reductase

Source
  • homo sapiens (human)
  • synthetic construct (others)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN/IMMUNE SYSTEM / GPCR / H2R / Histamine Receptor / MEMBRANE PROTEIN-IMMUNE SYSTEM complex / H3R

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