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 insights into how Yrb2p accelerates the assembly of the Xpo1p nuclear export complex.

Koyama M, Shirai N, Matsuura Y

Proteins and ribonucleoproteins containing a nuclear export signal (NES) assemble with the exportin Xpo1p (yeast CRM1) and Gsp1p-GTP (yeast Ran-GTP) in the nucleus and exit through the nuclear pore complex. In the cytoplasm, Yrb1p (yeast RanBP1) displaces NES from Xpo1p. Efficient export of NES-cargoes requires Yrb2p (yeast RanBP3), a primarily nuclear protein containing nucleoporin-like phenylalanine-glycine (FG) repeats and a low-affinity ... [more]

Cell Rep Nov. 06, 2014; 9(3);983-95 [Pubmed: 25437554]

Throughput

Low Throughput

Additional Notes

Co-crystal structure of human PKIA with yeast GSP1 and CRM1/XPO1.

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
CRM1 PKIA	Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.	Koyama M (2010)	Low	-	BioGRID	445418

Curated By

BioGRID

Interaction Summary

PKIA

Gene Ontology Biological Process

Gene Ontology Molecular Function

cAMP-dependent protein kinase inhibitor activity [IDA, TAS]protein binding [IPI]protein kinase A catalytic subunit binding [IPI]

Gene Ontology Cellular Component

CRM1