Linked Life Data

8841553

Source:http://linkedlifedata.com/resource/pubmed/id/8841553

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
1996-12-18
pubmed:abstractText
The purine repressor (PurR) consists of two functional domains: an N-terminal DNA-binding domain and a C-terminal corepressor-binding domain. Recently, the structure of PurR-corepressor-operator ternary complex was determined by X-ray crystallography. In the complex the DNA-binding domain, consisting of 56 amino acids, was composed of four helices. Here, we have determined the solution structure of the DNA-binding domain in its DNA free state by NMR. It consists of three helices and the fourth helix (the hinge helix) region is diordered. The architecture of the first three helices of its DNA free state is very similar to that of its DNA-bound form. The hinge helix is induced by the specific DNA binding and by the dimerization of PurR which is provided by the corepressor-binding domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0261-3166
pubmed:author
pubmed:issnType
Print
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
63-4
pubmed:dateRevised
2004-12-3
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Conformational changes of purine repressor DNA-binding domain upon complexation with DNA.
pubmed:affiliation
Graduate School of Integrated Science, Yokohama City University, Japan.
pubmed:publicationType
Journal Article