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- Title
The Crystal Structure of the Dachshund Domain of Human SnoN Reveals Flexibility in the Putative Protein Interaction Surface.
- Authors
Nyman, Tomas; Trésaugues, Lionel; Welin, Martin; Lehtiö, Lari; Flodin, Susanne; Persson, Camilla; Johansson, Ida; Hammarström, Martin; Nordlund, Pär
- Abstract
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 (http://plosone.org/enhanced/pone.0012907/) 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.
- Subjects
PROTEINS; HISTONE deacetylase; AMIDASES; DACHSHUNDS; HOMOLOGY (Biology); MONOMERS; MATERIAL plasticity; HOUNDS; CHEMICALS
- Publication
PLoS ONE, 2010, Vol 5, Issue 9, p1
- ISSN
1932-6203
- Publication type
Article
- DOI
10.1371/journal.pone.0012907