BAIT
ACTA1
ACTA, ASMA, CFTD, CFTD1, CFTDM, MPFD, NEM1, NEM2, NEM3, RP5-1068B5.2
actin, alpha 1, skeletal muscle
GO Process (4)
GO Function (5)
GO Component (9)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
CCT4
CCT-DELTA, Cctd, SRB
chaperonin containing TCP1, subunit 4 (delta)
GO Process (3)
GO Function (2)
GO Component (6)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Co-crystal Structure
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
Analysis of the interaction between the eukaryotic chaperonin CCT and its substrates actin and tubulin.
Two mechanisms have thus far been characterized for the assistance by chaperonins of the folding of other proteins. The first and best described is that of the prokaryotic chaperonin GroEL, which interacts with a large spectrum of proteins. GroEL uses a nonspecific mechanism by which any conformation of practically any unfolded polypeptide interacts with it through exposed, hydrophobic residues. ATP ... [more]
J. Struct. Biol. Aug. 01, 2001; 135(2);205-18 [Pubmed: 11580270]
Throughput
- Low Throughput
Curated By
- BioGRID