ArticleBiochemistry and biophysics reports2015
Model structures of inactive and peptide agonist bound C5aR: Insights into agonist binding, selectivity and activation.
Article in Biochemistry and biophysics reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Deciphering the conformational landscape of few selected aromatic noncoded amino acids (NCAAs) for applications in rational design of peptide therapeutics.Amino acids · 2022Article
- Binding of raloxifene to human complement fragment 5a (Journal of biomolecular structure & dynamics · 2022Article
- The Structural Basis of Peptide Binding at Class A G Protein-Coupled Receptors.Molecules (Basel, Switzerland) · 2021Review
- Interaction of Human C5a with the Major Peptide Fragments of C5aR1: Direct Evidence in Support of "Two-Site" Binding Paradigm.ACS omega · 2021Article
- Allosteric interactions in the parathyroid hormone GPCR-arrestin complex formation.Nature chemical biology · 2020Article
- The Model Structures of the Complement Component 5a Receptor (C5aR) Bound to the Native and EngineeredScientific reports · 2018Article
- Identification of novel natural compound inhibitors for human complement component 5a receptor by homology modeling and virtual screening.Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agentsArticle
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
C5a receptor (C5aR) is one of the major chemoattractant receptors of the druggable proteome that binds C5a, the proinflammatory polypeptide of complement cascade, triggering inflammation and SEPSIS. Here, we report the model structures of C5aR in both inactive and peptide agonist (YSFKPMPLaR; a=D-Ala) bound meta-active state. Assembled in CYANA and evolved over molecular dynamics (MD) in POPC bilayer, the inactive C5aR demonstrates a topologically unique compact heptahelical bundle topology harboring a β-hairpin in extracellular loop 2 (ECL2), derived from the atomistic folding simulations. The peptide agonist bound meta-active C5aR deciphers the "site2" at an atomistic resolution in the extracellular surface (ECS), in contrast to the previously hypothesized inter-helical crevice. With estimated Ki≈2.75 μM, the meta-active C5aR excellently rationalizes the IC
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.