Source:http://linkedlifedata.com/resource/pubmed/id/20957027
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
|
pubmed:dateCreated |
2010-10-19
|
pubmed:abstractText |
The human SnoN is an oncoprotein that interacts with several transcription-regulatory proteins such as the histone-deacetylase, N-CoR containing co-repressor complex and Smad proteins. This study presents the crystal structure of the Dachshund homology domain of human SnoN. The structure reveals a groove composed of conserved residues with characteristic properties of a protein-interaction surface. A comparison of the 12 monomers in the asymmetric unit reveals the presence of two major conformations: an open conformation with a well accessible groove and a tight conformation with a less accessible groove. The variability in the backbone between the open and the tight conformations matches the differences seen in previously determined structures of individual Dachshund homology domains, suggesting a general plasticity within this fold family. The flexibility observed in the putative protein binding groove may enable SnoN to recognize multiple interaction partners. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
1932-6203
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:volume |
5
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
e12907
|
pubmed:meshHeading |
pubmed-meshheading:20957027-Amino Acid Sequence,
pubmed-meshheading:20957027-Crystallography, X-Ray,
pubmed-meshheading:20957027-Humans,
pubmed-meshheading:20957027-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:20957027-Models, Molecular,
pubmed-meshheading:20957027-Molecular Conformation,
pubmed-meshheading:20957027-Molecular Sequence Data,
pubmed-meshheading:20957027-Protein Binding,
pubmed-meshheading:20957027-Protein Structure, Tertiary,
pubmed-meshheading:20957027-Proto-Oncogene Proteins,
pubmed-meshheading:20957027-Sequence Alignment
|
pubmed:year |
2010
|
pubmed:articleTitle |
The crystal structure of the Dachshund domain of human SnoN reveals flexibility in the putative protein interaction surface.
|
pubmed:affiliation |
Structural Genomics Consortium, Karolinska Institutet, Stockholm, Sweden. tomas.nyman@ki.se
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|