Linked Life Data

19170764

Source:http://linkedlifedata.com/resource/pubmed/id/19170764

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-1-27
pubmed:abstractText
The BTB/POZ domain is known as a protein-protein interaction motif that mediates homodimer and higher order self-associations. Proteins containing the BTB domain exist throughout eukaryotes; however, there is little information about the mechanism that determines the oligomeric state of the BTB domain. To address this question, we have determined the X-ray structure of the mouse Bach1 BTB domain. The present structure is similar to the previously determined BTB domain folds, including the human Bach1 BTB domain; however, distinct structural features are present, such as a novel homodimer interaction surface. The homodimer formation was found to involve a novel hydrogen bond network and interactions between hydrophobic surfaces of the kinked N-terminus (N-hook) and the partner's C-terminal residues. The deletion of the N-hook resulted in the conversion of the homodimer into a monomer in solution, indicating that the N-hook promotes the homodimerization of the mBach1 BTB domain. We have also found that the BTB domain of Bach2, a protein highly related to Bach1, is present as a monomer due to a short peptide insertion at the N-hook. These results represent the first example of the key modulatory element of BTB domain homodimerization.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1365-2443
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
167-78
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Crystal structure of the Bach1 BTB domain and its regulation of homodimerization.
pubmed:affiliation
Biomedical Engineering Research Organization, Tohoku University, Aoba-ku, Sendai, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't