The crystal structure of the Dachshund domain of human SnoN reveals flexibility in the putative protein interaction surface.

• Main Authors: Tomas Nyman, Lionel Trésaugues, Martin Welin, Lari Lehtiö, Susanne Flodin, Camilla Persson, Ida Johansson, Martin Hammarström, Pär Nordlund
• Format: Article
• Language: English
• Published: Public Library of Science (PLoS) 2010-09-01
• Series: PLoS ONE
• Online Access: http://europepmc.org/articles/PMC2944819?pdf=render

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.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.