The TLQP-21 peptide activates the G-protein-coupled receptor C3aR1 via a folding-upon-binding mechanism

Cheryl Cero, Vitaly V. Vostrikov, Raffaello Verardi, Cinzia Severini, Tata Gopinath, Patrick D. Braun, Maria F. Sassano, Allison Gurney, Bryan L. Roth, Lucy Vulchanova, Roberta Possenti, Gianluigi Veglia, Alessandro Bartolomucci

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

TLQP-21, a VGF-encoded peptide is emerging as a novel target for obesity-associated disorders. TLQP-21 is found in the sympathetic nerve terminals in the adipose tissue and targets the G-protein-coupled receptor complement-3a receptor1 (C3aR1). The mechanisms of TLQP-21-induced receptor activation remain unexplored. Here, we report that TLQP-21 is intrinsically disordered and undergoes a disorder-to-order transition, adopting an α-helical conformation upon targeting cells expressing the C3aR1. We determined that the hot spots for TLQP-21 are located at the C terminus, with mutations in the last four amino acids progressively reducing the bioactivity and, a single site mutation (R21A) or C-terminal amidation abolishing its function completely. Additionally, the human TLQP-21 sequence carrying a S20A substitution activates the human C3aR1 receptor with lower potency compared to the rodent sequence. These studies reveal the mechanism of action of TLQP-21 and provide molecular templates for designing agonists and antagonists to modulate C3aR1 functions.

Original languageEnglish (US)
Pages (from-to)1744-1753
Number of pages10
JournalStructure
Volume22
Issue number12
DOIs
StatePublished - Dec 2 2014

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© 2014 Elsevier Ltd. All rights reserved.

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