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

Model of interaction of the IL-1 receptor accessory protein IL-1RAcP with the IL-1beta/IL-1R(I) complex.

FEBS letters - 15 Jun 2001

Casadio R, Frigimelica E, Bossù P, Neumann D, Martin M U, Tagliabue A, Boraschi D

Abstract excerpt

A preliminary model has been calculated for the activating interaction of the interleukin 1 receptor (IL-1R) accessory protein IL-1RAcP with the ligand/receptor complex IL-1beta/IL-1R(I). First, IL-1RAcP was modeled on the crystal structure of IL-1R(I) bound to IL-1beta. Then, the IL-1RAcP model was docked using specific programs to the crystal structure of the IL-1beta/IL-1R(I) complex. Two types of models were...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies
Share to Antibody Specificity
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Interleukin-1

Share to Rabbits

Share to Receptors, Interleukin-1

Share to T-Lymphocytes

Share to Thymus Gland

Source

Identifiers

PMID: 11418113
DOI: 10.1016/s0014-5793(01)02515-7

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Model of interaction of the IL-1 receptor accessory protein IL-1RAcP with the IL-1beta/IL-1R(I) complex.PMID 11418113Read ↗

Structural biology of the IL‐1 superfamily: Key cytokines in the regulation of immune and inflammatory responsesSemantic proximity Read ↗

IL-1 Family Cytokines Use Distinct Molecular Mechanisms to Signal through Their Shared Co-receptor.Semantic proximity Read ↗

Optimization of IL-1Ra Structure to Achieve a Smaller Protein with a Higher Affinity to its ReceptorSemantic proximity Read ↗

Identification of essential regions in the cytoplasmic tail of interleukin-1 receptor accessory protein critical for interleukin-1 signaling.Semantic proximity Read ↗

Interactive sites in the MyD88 Toll/interleukin (IL) 1 receptor domain responsible for coupling to the IL1beta signaling pathway.Semantic proximity Read ↗

The interleukin‐1 family: 10 years of discovery 1Semantic proximity Read ↗

Identification of critical regions within the TIR domain of IL-1 receptor type I.Semantic proximity Read ↗

Refined crystal structure of the interleukin-1 receptor antagonist. Presence of a disulfide link and a cis-proline.Semantic proximity Read ↗

Structure and function of chicken interleukin-1 beta mutants: uncoupling of receptor binding and in vivo biological activity.Semantic proximity Read ↗

Direct binding to integrins and loss of disulfide linkage in interleukin-1β (IL-1β) are involved in the agonistic action of IL-1β.Semantic proximity Read ↗

Inhibitory activity of IL-1 receptor antagonist depends on the balance between binding capacity for IL-1 receptor type 1 and IL-1 receptor type II.Semantic proximity Read ↗

A novel mutation in the interleukin-1 receptor antagonist associated with intrauterine disease onset.Semantic proximity Read ↗

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