A combination of structural, biochemical, and genetic studies in model organisms was used to infer a cellular role for the human protein (SBDS) responsible for Shwachman-Bodian-Diamond syndrome. The crystal structure of the SBDS homologue in Archaeoglobus fulgidus, AF0491, revealed a three domain protein. The N-terminal domain, which harbors the majority of disease-linked mutations, has a novel three-dimensional fold.
Revised: July 19, 2005 |
Published: May 13, 2005
Citation
Savchenko A., N. Krogan, J.R. Cort, E. Evdokimova, J.M. Lew, A. Yee, and L. Sanchez-Pulido, et al. 2005.The Shwachman-Bodian-Diamond Syndrome Protein Family Is Involved in RNA Metabolism.Journal of Biological Chemistry 280, no. 19:19213-19220.PNNL-SA-45303.doi:10.1074/jbc.M414421200