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

Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains.

Misra S, Puertollano R, Kato Y, Bonifacino JS, Hurley JH

Specific sorting signals direct transmembrane proteins to the compartments of the endosomal-lysosomal system. Acidic-cluster-dileucine signals present within the cytoplasmic tails of sorting receptors, such as the cation-independent and cation-dependent mannose-6-phosphate receptors, are recognized by the GGA (Golgi-localized, gamma-ear-containing, ADP-ribosylation-factor-binding) proteins. The VHS (Vps27p, Hrs and STAM) domains of the GGA proteins are responsible for the highly specific recognition of these ... [more]

Nature Feb. 21, 2002; 415(6874);933-7 [Pubmed: 11859375]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
M6PR GGA3	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	Puertollano R (2001)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

GGA3

Gene Ontology Biological Process

Gene Ontology Molecular Function

ADP-ribosylation factor binding [IDA]protein binding [IPI]

Gene Ontology Cellular Component

M6PR