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TitleStructural basis of neuropeptide Y signaling through Y and Y receptors.
Journal, issue, pagesMedComm (2020), Vol. 5, Issue 7, Page e565, Year 2024
Publish dateJun 15, 2024
AuthorsSiyuan Shen / Yue Deng / Chenglong Shen / Haidi Chen / Lin Cheng / Chao Wu / Chang Zhao / Zhiqian Yang / Hanlin Hou / Kexin Wang / Zhenhua Shao / Cheng Deng / Feng Ye / Wei Yan /
PubMed AbstractNeuropeptide Y (NPY), a 36-amino-acid peptide, functions as a neurotransmitter in both the central and peripheral nervous systems by activating the NPY receptor subfamily. Notably, NPY analogs ...Neuropeptide Y (NPY), a 36-amino-acid peptide, functions as a neurotransmitter in both the central and peripheral nervous systems by activating the NPY receptor subfamily. Notably, NPY analogs display varying selectivity and exert diverse physiological effects through their interactions with this receptor family. [Pro]-NPY and [Leu, Pro]-NPY, mainly acting on YR, reportedly increases blood pressure and postsynaptically potentiates the effect of other vasoactive substances above all, while N-terminal cleaved NPY variants in human body primary mediates angiogenesis and neurotransmitter release inhibition through YR. However, the recognition mechanisms of YR and YR with specific agonists remain elusive, thereby hindering subtype receptor-selective drug development. In this study, we report three cryo-electron microscopy (cryo-EM) structures of Gi2-coupled YR and YR in complexes with NPY, as well as YR bound to a selective agonist [Leu, Pro]-NPY. Combined with cell-based assays, our study not only reveals the conserved peptide-binding mode of NPY receptors but also identifies an additional sub-pocket that confers ligand selectivity. Moreover, our analysis of YR evolutionary dynamics suggests that this sub-pocket has undergone functional adaptive evolution across different species. Collectively, our findings shed light on the molecular underpinnings of neuropeptide recognition and receptor activation, and they present a promising avenue for the design of selective drugs targeting the NPY receptor family.
External linksMedComm (2020) / PubMed:38882210 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 3.3 Å
Structure data

36923

8k6m

EMDB-36923, PDB-8k6m:
Structural complex of neuropeptide Y receptor 1
Method: EM (single particle) / Resolution: 3.3 Å

36924

8k6n

EMDB-36924, PDB-8k6n:
Structural complex of neuropeptide Y receptor 2
Method: EM (single particle) / Resolution: 3.2 Å

36925

8k6o

EMDB-36925, PDB-8k6o:
Structural complex of neuropeptide Y receptor 1
Method: EM (single particle) / Resolution: 3.3 Å

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / neuropeptide Y receptor 1 / complex / neuropeptide Y receptor 2

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