Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

A new cytokine-receptor binding mode revealed by the crystal structure of the IL-1 receptor with an antagonist.

Schreuder H, Tardif C, Trump-Kallmeyer S, Soffientini A, Sarubbi E, Akeson A, Bowlin T, Yanofsky S, Barrett RW

Inflammation, regardless of whether it is provoked by infection or by tissue damage, starts with the activation of macrophages which initiate a cascade of inflammatory responses by producing the cytokines interleukin-1 (IL-1) and tumour necrosis factor-alpha (ref. 1). Three naturally occurring ligands for the IL-1 receptor (IL1R) exist: the agonists IL-1alpha and IL-1beta and the IL-1-receptor antagonist IL1RA (ref. 2). ... [more]

Nature Mar. 13, 1997; 386(6621);194-200 [Pubmed: 9062194]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
IL1R1 IL1RN	Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.	Huttlin EL (2021)	High	1	BioGRID	3155389

Curated By

BioGRID

Interaction Summary

IL1R1

Gene Ontology Biological Process

Gene Ontology Molecular Function

interleukin-1 receptor activity [IDA]platelet-derived growth factor receptor binding [IPI]protein binding [IPI]signal transducer activity [TAS]transmembrane signaling receptor activity [TAS]

Gene Ontology Cellular Component

IL1RN