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

Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of the adhesion protein ICAM-2.

Hamada K, Shimizu T, Matsui T, Tsukita S, Tsukita S, Hakoshima T

Radixin is a member of the ERM proteins, which cross-link plasma membranes and actin filaments. The FERM domains located at the N-terminal regions of ERM proteins are responsible for membrane association through direct interactions with the cytoplasmic domains of integral membrane proteins. Here, crystals of the complex between the radixin FERM domain and the full-length cytoplasmic tail (28-residue peptide) of ... [more]

Acta Crystallogr. D Biol. Crystallogr. Jun. 01, 2001; 57(0);891-2 [Pubmed: 11375520]

Throughput

Low Throughput

Curated By

BioGRID

Interaction Summary

RDX

Gene Ontology Biological Process

Gene Ontology Molecular Function

poly(A) RNA binding [IDA]protein binding [IPI]

Gene Ontology Cellular Component

ICAM2