Shwachman-Bodian-Diamond Syndrome Protein

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Simmi Parhar
Simmi Parhar
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== '''Shwachman-Bodian-Diamond Syndrome Protein''' ==
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= '''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>PMID:15701631</ref><ref>PMID:15701634</ref>. Evidence has been provided that the SBDS protein orthologues may play a role in RNA metabolism <ref>PMID:15701631</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>PMID:19121363</ref>. The resolution of the Archaeoglobulus fulgidus SBDS protein orthologue is at a resolution of 1.9 angstroms; showcasing a three domain architecture <ref>PMID: 15701631</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>PMID:15701631</ref>.
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{{STRUCTURE_1t95 | PDB=1T95 | SCENE=}}
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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>PMID: 15701631</ref><ref>PMID: 15701634</ref>. Evidence has been provided that the SBDS protein orthologues may play a role in RNA metabolism <ref>PMID: 15701631<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>PMID: 19121363<ref>. The resolution of the Archaeoglobulus fulgidus SBDS protein orthologue is at a resolution of 1.9 angstroms; showcasing a three domain architecture <ref>PMID: 15701631<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>PMID: 15701631<ref>.
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=References=
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Revision as of 20:51, 25 March 2010

Simmi Parhar

Shwachman-Bodian-Diamond Syndrome Protein

OVERVIEW

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 [1][2]. Evidence has been provided that the SBDS protein orthologues may play a role in RNA metabolism [3]. 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 [4]. The resolution of the Archaeoglobulus fulgidus SBDS protein orthologue is at a resolution of 1.9 angstroms; showcasing a three domain architecture [5]. 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 [6]. Template:STRUCTURE 1t95

References

  1. ↑ Shammas C, Menne TF, Hilcenko C, Michell SR, Goyenechea B, Boocock GR, Durie PR, Rommens JM, Warren AJ. Structural and mutational analysis of the SBDS protein family. Insight into the leukemia-associated Shwachman-Diamond Syndrome. J Biol Chem. 2005 May 13;280(19):19221-9. Epub 2005 Feb 8. PMID:15701631 doi:http://dx.doi.org/10.1074/jbc.M414656200
  2. ↑ Savchenko A, Krogan N, Cort JR, Evdokimova E, Lew JM, Yee AA, Sanchez-Pulido L, Andrade MA, Bochkarev A, Watson JD, Kennedy MA, Greenblatt J, Hughes T, Arrowsmith CH, Rommens JM, Edwards AM. The Shwachman-Bodian-Diamond syndrome protein family is involved in RNA metabolism. J Biol Chem. 2005 May 13;280(19):19213-20. Epub 2005 Feb 8. PMID:15701634 doi:10.1074/jbc.M414421200
  3. ↑ Shammas C, Menne TF, Hilcenko C, Michell SR, Goyenechea B, Boocock GR, Durie PR, Rommens JM, Warren AJ. Structural and mutational analysis of the SBDS protein family. Insight into the leukemia-associated Shwachman-Diamond Syndrome. J Biol Chem. 2005 May 13;280(19):19221-9. Epub 2005 Feb 8. PMID:15701631 doi:http://dx.doi.org/10.1074/jbc.M414656200
  4. ↑ de Oliveira JF, Castilho BA, Sforca ML, Krieger MA, Zeri AC, Guimaraes BG, Zanchin NI. Characterization of the Trypanosoma cruzi ortholog of the SBDS protein reveals an intrinsically disordered extended C-terminal region showing RNA-interacting activity. Biochimie. 2009 Apr;91(4):475-83. Epub 2008 Dec 16. PMID:19121363 doi:10.1016/j.biochi.2008.12.001
  5. ↑ Shammas C, Menne TF, Hilcenko C, Michell SR, Goyenechea B, Boocock GR, Durie PR, Rommens JM, Warren AJ. Structural and mutational analysis of the SBDS protein family. Insight into the leukemia-associated Shwachman-Diamond Syndrome. J Biol Chem. 2005 May 13;280(19):19221-9. Epub 2005 Feb 8. PMID:15701631 doi:http://dx.doi.org/10.1074/jbc.M414656200
  6. ↑ Shammas C, Menne TF, Hilcenko C, Michell SR, Goyenechea B, Boocock GR, Durie PR, Rommens JM, Warren AJ. Structural and mutational analysis of the SBDS protein family. Insight into the leukemia-associated Shwachman-Diamond Syndrome. J Biol Chem. 2005 May 13;280(19):19221-9. Epub 2005 Feb 8. PMID:15701631 doi:http://dx.doi.org/10.1074/jbc.M414656200
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