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

Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.

Pearson MA, Reczek D, Bretscher A, Karplus PA

The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding segment and an N-terminal FERM domain, a common membrane binding module. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites. The crystal structure of a dormant moesin FERM/tail ... [more]

Cell Apr. 28, 2000; 101(3);259-70 [Pubmed: 10847681]

Throughput

Low Throughput

Additional Notes

domain-domain contacts

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
MSN MSN	Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).	Yugandhar K (2020)	High	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

MSN

Gene Ontology Biological Process

Gene Ontology Molecular Function

cell adhesion molecule binding [IPI]double-stranded RNA binding [IDA]protein binding [IPI]protein kinase binding [IPI]receptor binding [IPI]structural constituent of cytoskeleton [TAS]

Gene Ontology Cellular Component

MSN