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

Crystal structure of the alpha-actinin rod reveals an extensive torsional twist.

Ylaenne J, Scheffzek K, Young P, Saraste M

BACKGROUND: Alpha-actinin is a ubiquitously expressed protein found in numerous actin structures. It consists of an N-terminal actin binding domain, a central rod domain, and a C-terminal domain and functions as a homodimer to cross-link actin filaments. The rod domain determines the distance between cross-linked actin filaments and also serves as an interaction site for several cytoskeletal and signaling proteins. ... [more]

Structure Jul. 03, 2001; 9(7);597-604 [Pubmed: 11470434]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
ACTN1 ACTN1	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.	Rolland T (2014)	High	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

ACTN1

Gene Ontology Biological Process

Gene Ontology Molecular Function

double-stranded RNA binding [IDA]integrin binding [IDA]ion channel binding [IPI]protein binding [IPI]vinculin binding [IPI]

Gene Ontology Cellular Component