Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Asymmetric usage of antagonist charged residues drives interleukin-5 receptor recruitment but is insufficient for receptor activation.

Biochemistry - 31 Jan 2006

Ishino Tetsuya, Pillalamarri Udaya, Panarello Dominick, Bhattacharya Madhushree, Urbina Cecilia, Horvat Stephanie, Sarkhel Sanjay, Jameson Bradford, Chaiken Irwin

Abstract excerpt

The cyclic peptide AF17121 (VDECWRIIASHTWFCAEE) is a library-derived antagonist for human Interleukin-5 receptor alpha (IL5Ralpha). We have previously demonstrated that AF17121 mimics Interleukin-5 (IL5) by binding in a region of IL5Ralpha that overlaps the IL5 binding epitope. In the present study, to explore the functional importance of the amino acid residues of AF17121 required for effective binding to, and...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Arginine
Share to Epitopes

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histidine

Share to Peptides, Cyclic

Share to Receptors, Interleukin

Share to Structure-Activity Relationship

Share to Surface Plasmon Resonance

Share to Thioredoxins

Source

Open in PubMed Open full text

Identifiers

PMID: 16430207
DOI: 10.1021/bi0518038
PMCID: PMC2538410

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Asymmetric usage of antagonist charged residues drives interleukin-5 receptor recruitment but is insufficient for receptor activation.PMID 16430207Read ↗

AF12198, a Novel Low Molecular Weight Antagonist, Selectively Binds the Human Type I Interleukin (IL)-1 Receptor and Blocks in Vivo Responses to IL-1Semantic proximity Read ↗

Kinetic interaction analysis of human interleukin 5 receptor alpha mutants reveals a unique binding topology and charge distribution for cytokine recognition.Semantic proximity Read ↗

Functional Role of the C-Terminal Amphipathic Helix 8 of Olfactory Receptors and Other G Protein-Coupled Receptors.Semantic proximity Read ↗

Arginine 206 of the C5a receptor is critical for ligand recognition and receptor activation by C-terminal hexapeptide analogs.Semantic proximity Read ↗

Modulation of the agonist and antagonist activity of peptidic FPR1 ligands through N-terminal modifications: A structural and functional analysisSemantic proximity Read ↗

Molecular mechanism of naturally-encoded signaling-bias at the complement anaphylatoxin receptorsSemantic proximity Read ↗

Ligand-mimicking receptor variant discloses binding and activation mode of prolactin-releasing peptide.Semantic proximity Read ↗

A mixed-charge pair in human interleukin 4 dominates high-affinity interaction with the receptor alpha chain.Semantic proximity Read ↗

Structural basis of <i>γ</i> -chain family receptor sharing at the membrane levelSemantic proximity Read ↗

C5a receptor activation. Genetic identification of critical residues in four transmembrane helices.Semantic proximity Read ↗

A surface-exposed region of G(salpha) in which substitutions decrease receptor-mediated activation and increase receptor affinity.Semantic proximity Read ↗

A modular interface of IL-4 allows for scalable affinity without affecting specificity for the IL-4 receptor.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.