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PDBsum entry 7d3s
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Membrane protein
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PDB id
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7d3s
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Contents |
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27 a.a.
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266 a.a.
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230 a.a.
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340 a.a.
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57 a.a.
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128 a.a.
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References listed in PDB file
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Key reference
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Title
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Structure of the human secretin receptor coupled to an engineered heterotrimeric g protein.
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Authors
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S.Fukuhara,
K.Kobayashi,
T.Kusakizako,
W.Iida,
M.Kato,
W.Shihoya,
O.Nureki.
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Ref.
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Biochem Biophys Res Commun, 2020,
533,
861-866.
[DOI no: ]
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PubMed id
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Abstract
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Secretin is a gastrointestinal hormone that exerts multiple physiological
functions via activation of the secretin receptor (SECR). SECR belongs to the
class B G-protein-coupled receptors and is involved in various processes, such
as regulation of the pH of the duodenal content, food intake, and water
homeostasis. Here, we report a cryo-electron microscopy structure of human SECR
bound to secretin and an engineered Gs heterotrimer. The structure revealed the
basic architecture of SECR and the secretin binding mode. A structural
comparison of the SECR and PAC1R transmembrane domains revealed that
transmembrane helices 1 and 2 play a prominent role in secretin recognition.
Moreover, the extracellular domain of SECR is perpendicular to the TMD, unlike
that of PAC1R. This comparison revealed the diverged peptide recognition
mechanisms of these receptors, which belong to the same subgroup. Our structural
information will facilitate drug discovery research for clinical applications.
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