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TitleCryo-EM structure of the human histamine H receptor/G complex.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 2086, Year 2021
Publish dateApr 7, 2021
AuthorsRuixue Xia / Na Wang / Zhenmei Xu / Yang Lu / Jing Song / Anqi Zhang / Changyou Guo / Yuanzheng He /
PubMed AbstractHistamine receptors play important roles in various pathophysiological conditions and are effective targets for anti-allergy treatment, however the mechanism of receptor activation remain elusive. ...Histamine receptors play important roles in various pathophysiological conditions and are effective targets for anti-allergy treatment, however the mechanism of receptor activation remain elusive. Here, we present the cryo-electron microscopy (cryo-EM) structure of the human HR in complex with a G protein in an active conformation via a NanoBiT tethering strategy. The structure reveals that histamine activates receptor via interacting with the key residues of both transmembrane domain 3 (TM3) and TM6 to squash the binding pocket on the extracellular side and to open the cavity on the intracellular side for G engagement in a model of "squash to activate and expand to deactivate". The structure also reveals features for G coupling, including the interaction between intracellular loop 2 (ICL2) and the αN-β junction of G protein. The detailed analysis of our structure will provide a framework for understanding G-protein coupling selectivity and clues for designing novel antihistamines.
External linksNat Commun / PubMed:33828102 / PubMed Central
MethodsEM (single particle)
Resolution3.3 Å
Structure data

30665

7dfl

EMDB-30665, PDB-7dfl:
Cryo-EM structure of histamine H1 receptor Gq complex
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-HSM:
HISTAMINE / neurotransmitter, hormone*YM

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / complex

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