The cDNA-derived amino acid sequence of chick heat shock protein Mr 90,000 (HSP 90) reveals a "DNA like" structure: potential site of interaction with steroid receptors.
We report cDNA sequence, the complete derived aa sequence, and a predicted secondary structure of the chick hsp 90, a protein which has been found to form complexes with steroid hormone receptors. The modelling of the most negatively charged "region A" indicates that the alpha-helices of this portion of hsp 90 mimick DNA configuration. We propose that this region can, in absence of hormone, interact with and cap the positively charged DNA-binding domain of steroid receptors.
Binart
N
N
Lab. Hormones, INSERM U 33, Bicêtre, France.
Chambraud
B
B
Dumas
B
B
Rowlands
D A
DA
Bigogne
C
C
Levin
J M
JM
Garnier
J
J
Baulieu
E E
EE
Catelli
M G
MG
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D002645:Chickens; D003001:Cloning, Molecular; D003062:Codon; D004247:DNA / Q000235:genetics / Q000302:isolation & purification; D015246:Deoxyribonuclease EcoRI; D005260:Female; D006031:Glycosylation; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009693:Nucleic Acid Hybridization; D010766:Phosphorylation; D011487:Protein Conformation; D011494:Protein Kinases / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid
D003062:Codon; D006360:Heat-Shock Proteins; D004247:DNA; D011494:Protein Kinases; D015246:Deoxyribonuclease EcoRI