Shwachman-Bodian-Diamond Syndrome Protein
From Proteopedia
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== '''Shwachman-Bodian-Diamond Syndrome Protein''' == | == '''Shwachman-Bodian-Diamond Syndrome Protein''' == | ||
== '''OVERVIEW''' == | == '''OVERVIEW''' == | ||
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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>. | ||
<references/> | <references/> | ||
Revision as of 04:13, 25 March 2010
| Please do NOT make changes to this Sandbox until after April 23, 2010. Sandboxes 151-200 are reserved until then for use by the Chemistry 307 class at UNBC taught by Prof. Andrea Gorrell. |
Proteopedia Page Contributors and Editors (what is this?)
Simmi Parhar, Jaime Prilusky, Michal Harel, Alexander Berchansky, David Canner, Andrea Gorrell
