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

Domain swap in the C-terminal ubiquitin-like domain of human doublecortin.

Rufer AC, Kusznir E, Burger D, Stihle M, Ruf A, Rudolph MG

Doublecortin, a microtubule-associated protein that is only produced during neurogenesis, cooperatively binds to microtubules and stimulates microtubule polymerization and cross-linking by unknown mechanisms. A domain swap is observed in the crystal structure of the C-terminal domain of doublecortin. As determined by analytical ultracentrifugation, an open conformation is also present in solution. At higher concentrations, higher-order oligomers of the domain are ... [more]

Acta Crystallogr D Struct Biol May. 01, 2018; 74(Pt 5);450-462 [Pubmed: 29717716]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
DCX DCX	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Caspi M (2000)	Low	-	BioGRID	-
DCX DCX	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Rufer AC (2018)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

DCX

Gene Ontology Biological Process

Gene Ontology Molecular Function

microtubule binding [IDA]protein binding [IPI]protein kinase binding [IPI]

Gene Ontology Cellular Component

DCX