Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-4-17
pubmed:databankReference
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
159
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
140-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:2923621-Amino Acid Sequence, pubmed-meshheading:2923621-Animals, pubmed-meshheading:2923621-Base Sequence, pubmed-meshheading:2923621-Binding Sites, pubmed-meshheading:2923621-Chickens, pubmed-meshheading:2923621-Cloning, Molecular, pubmed-meshheading:2923621-Codon, pubmed-meshheading:2923621-DNA, pubmed-meshheading:2923621-Deoxyribonuclease EcoRI, pubmed-meshheading:2923621-Female, pubmed-meshheading:2923621-Glycosylation, pubmed-meshheading:2923621-Heat-Shock Proteins, pubmed-meshheading:2923621-Humans, pubmed-meshheading:2923621-Molecular Sequence Data, pubmed-meshheading:2923621-Molecular Weight, pubmed-meshheading:2923621-Nucleic Acid Hybridization, pubmed-meshheading:2923621-Phosphorylation, pubmed-meshheading:2923621-Protein Conformation, pubmed-meshheading:2923621-Protein Kinases, pubmed-meshheading:2923621-Sequence Homology, Nucleic Acid
pubmed:year
1989
pubmed:articleTitle
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.
pubmed:affiliation
Lab. Hormones, INSERM U 33, Bicêtre, France.
pubmed:publicationType
Journal Article, Comparative Study