stranded anti-parallel-sheet. Central domain The function of this protein domain has been difficult to elucidate. It is possible that it has a role in binding to DNA or RNA. Protein binding to form a protein complex is also another possibility. It has been difficult to infer the function from the structure since this particular domain structure is found in archea. This domain contains a very common structure, the winged helix-turn-helix. C-terminal domain In molecular biology, the SBDS C-terminal protein domain is highly conserved in species ranging from archaea to vertebrates and plants. Members of this family are thought to play a role in RNA metabolism. However, its precise function remains to be elucidated. Furthermore, its structure makes it very difficult to predict the protein domain's function. The structure of the C-terminal domain contains a ferredoxin-like fold This structure has a four-stranded beta-sheet with two helices on one side. Clinical significance Mutations within this gene are associated with Shwachman-Bodian-Diamond syndrome. The two most common mutations associated with this syndrome are at positions 183–184 (TA→CT) resulting in a premature stop-codon (K62X) and a frameshift mutation at position 258 (2T→C) resulting in a stopcodon (C84fsX3). References Further reading External links GeneReviews/NIH/NCBI/UW entry on Shwachman-Diamond Syndrome