Shwachman-Bodian-Diamond Syndrome Protein

The human Shwachman-Bodian-Diamond syndrome(SBDS) protein belongs to a very conserved family of proteins of unknown function; orthologues found in Archaea, as well as plants and other eukaryotes <ref>1<ref>. Evidence has been provided that the SBDS protein orthologues may play a role in RNA metabolism <ref>1<ref>. Two groups of SBDS orthologues have been identified. Archaea, animals, and fungi have SBDS proteins with approximately 250 amino acid residues. However, SBDS protein of plants and protists has the C-terminal extensions around 100 to 250 amino acid residues <ref>3<ref>. The resolution of the Archaeoglobulus fulgidus SBDS protein orthologue is at a resolution of 1.9 angstroms; showcasing a three domain architecture <ref>4<ref>. The domain that is the most targeted for disease mutations is the N-terminal domain; containing a mixed alpha/beta fold. The central domain has a three-helical bundle, and the C-terminal domain has a ferredoxin-like fold <ref>4<ref>.

The human Shwachman-Bodian-Diamond syndrome(SBDS) protein belongs to a very conserved family of proteins of unknown function; orthologues found in Archaea, as well as plants and other eukaryotes <ref>1<ref>. Evidence has been provided that the SBDS protein orthologues may play a role in RNA metabolism <ref>1<ref>. Two groups of SBDS orthologues have been identified. Archaea, animals, and fungi have SBDS proteins with approximately 250 amino acid residues. However, SBDS protein of plants and protists has the C-terminal extensions around 100 to 250 amino acid residues <ref>3<ref>. The resolution of the Archaeoglobulus fulgidus SBDS protein orthologue is at a resolution of 1.9 angstroms; showcasing a three domain architecture <ref>4<ref>. The domain that is the most targeted for disease mutations is the N-terminal domain; containing a mixed alpha/beta fold. The central domain has a three-helical bundle, and the C-terminal domain has a ferredoxin-like fold <ref>4<ref>.

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