View source for 2kdo

{{Large structure}}
==Structure of the human Shwachman-Bodian-Diamond syndrome protein, SBDS==
<StructureSection load='2kdo' size='340' side='right' caption='[[2kdo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2kdo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KDO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KDO FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SBDS, CGI-97 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2kdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kdo OCA], [http://pdbe.org/2kdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kdo RCSB], [http://www.ebi.ac.uk/pdbsum/2kdo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kdo ProSAT]</span></td></tr>
</table>
{{Large structure}}
== Disease ==
[[http://www.uniprot.org/uniprot/SBDS_HUMAN SBDS_HUMAN]] Idiopathic aplastic anemia;Shwachman-Diamond syndrome. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:21536732</ref> <ref>PMID:12496757</ref>  
== Function ==
[[http://www.uniprot.org/uniprot/SBDS_HUMAN SBDS_HUMAN]] Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFTUD1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation.<ref>PMID:17643419</ref> <ref>PMID:19602484</ref> <ref>PMID:19759903</ref> <ref>PMID:21536732</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kd/2kdo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2kdo ConSurf].
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== Publication Abstract from PubMed ==
Shwachman-Bodian-Diamond syndrome is an autosomal recessive genetic syndrome with pleiotropic phenotypes, including pancreatic deficiencies, bone marrow dysfunctions with increased risk of myelodysplasia or leukemia, and skeletal abnormalities. This syndrome has been associated with mutations in the SBDS gene, which encodes a conserved protein showing orthologs in Archaea and eukaryotes. The Shwachman-Bodian-Diamond syndrome pleiotropic phenotypes may be an indication of different cell type requirements for a fully functional SBDS protein. RNA-binding activity has been predicted for archaeal and yeast SBDS orthologs, with the latter also being implicated in ribosome biogenesis. However, full-length SBDS orthologs function in a species-specific manner, indicating that the knowledge obtained from model systems may be of limited use in understanding major unresolved issues regarding SBDS function, namely, the effect of mutations in human SBDS on its biochemical function and the specificity of RNA interaction. We determined the solution structure and backbone dynamics of the human SBDS protein and describe its RNA binding site using NMR spectroscopy. Similarly to the crystal structures of Archaea, the overall structure of human SBDS comprises three well-folded domains. However, significant conformational exchange was observed in NMR dynamics experiments for the flexible linker between the N-terminal domain and the central domain, and these experiments also reflect the relative motions of the domains. RNA titrations monitored by heteronuclear correlation experiments and chemical shift mapping analysis identified a classic RNA binding site at the N-terminal FYSH (fungal, Yhr087wp, Shwachman) domain that concentrates most of the mutations described for the human SBDS.

Structure, dynamics, and RNA interaction analysis of the human SBDS protein.,de Oliveira JF, Sforca ML, Blumenschein TM, Goldfeder MB, Guimaraes BG, Oliveira CC, Zanchin NI, Zeri AC J Mol Biol. 2010 Mar 5;396(4):1053-69. Epub 2010 Jan 4. PMID:20053358<ref>PMID:20053358</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2kdo" style="background-color:#fffaf0;"></div>

==See Also==
*[[Shwachman-Bodian-Diamond Syndrome Protein|Shwachman-Bodian-Diamond Syndrome Protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Blumenschein, T]]
[[Category: Guimaraes, B G]]
[[Category: Oliveira, J F.de]]
[[Category: Sforca, M L]]
[[Category: Zanchin, N I.T]]
[[Category: Zeri, A C]]
[[Category: Disease mutation]]
[[Category: Nmr protein structure]]
[[Category: Phosphoprotein]]
[[Category: Ribosome biogenesis]]
[[Category: Rna binding protein]]
[[Category: Rna-interacting protein]]
[[Category: Sbds protein]]