3ucg
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of a RNA binding domain of polyadenylate-binding protein (PABPN1) from Homo sapiens at 1.95 A resolution== | |
- | + | <StructureSection load='3ucg' size='340' side='right' caption='[[3ucg]], [[Resolution|resolution]] 1.95Å' scene=''> | |
- | + | == Structural highlights == | |
- | ==Disease== | + | <table><tr><td colspan='2'>[[3ucg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UCG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UCG FirstGlance]. <br> |
- | [[http://www.uniprot.org/uniprot/PABP2_HUMAN PABP2_HUMAN]] Defects in PABPN1 are the cause of oculopharyngeal muscular dystrophy (OPMD) [MIM:[http://omim.org/entry/164300 164300]]. OPMD is a form of late-onset slowly progressive myopathy characterized by eyelid ptosis, dysphagia and, sometimes by other cranial and limb-muscle involvement.<ref>PMID:9462747</ref><ref>PMID:12673802</ref> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |
- | ==Function== | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BC010939, PAB2, PABP2, PABPN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
- | [[http://www.uniprot.org/uniprot/PABP2_HUMAN PABP2_HUMAN]] Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Is also present at various stages of mRNA metabolism including nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to synergistically activate E-box-mediated transcription through MYOD1 and may regulate the expression of muscle-specific genes. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation (By similarity).<ref>PMID:11689481</ref><ref>PMID:11371506</ref> | + | <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=3ucg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ucg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ucg RCSB], [http://www.ebi.ac.uk/pdbsum/3ucg PDBsum]</span></td></tr> |
- | + | </table> | |
- | == | + | == Disease == |
- | + | [[http://www.uniprot.org/uniprot/PABP2_HUMAN PABP2_HUMAN]] Defects in PABPN1 are the cause of oculopharyngeal muscular dystrophy (OPMD) [MIM:[http://omim.org/entry/164300 164300]]. OPMD is a form of late-onset slowly progressive myopathy characterized by eyelid ptosis, dysphagia and, sometimes by other cranial and limb-muscle involvement.<ref>PMID:9462747</ref> <ref>PMID:12673802</ref> | |
- | + | == Function == | |
- | + | [[http://www.uniprot.org/uniprot/PABP2_HUMAN PABP2_HUMAN]] Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Is also present at various stages of mRNA metabolism including nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to synergistically activate E-box-mediated transcription through MYOD1 and may regulate the expression of muscle-specific genes. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation (By similarity).<ref>PMID:11689481</ref> <ref>PMID:11371506</ref> | |
- | <references | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: TCELL, Partnership for T-Cell Biology | + | </StructureSection> |
+ | [[Category: Human]] | ||
+ | [[Category: Structural genomic]] | ||
+ | [[Category: TCELL, Partnership for T-Cell Biology]] | ||
[[Category: Ferredoxin-like]] | [[Category: Ferredoxin-like]] | ||
[[Category: Jcsg]] | [[Category: Jcsg]] | ||
- | [[Category: Joint center for structural genomic]] | ||
[[Category: Partnership for t-cell biology]] | [[Category: Partnership for t-cell biology]] | ||
- | [[Category: Protein structure initiative]] | + | [[Category: PSI, Protein structure initiative]] |
[[Category: Psi-biology]] | [[Category: Psi-biology]] | ||
[[Category: Rna binding protein]] | [[Category: Rna binding protein]] | ||
- | [[Category: Structural genomic]] | ||
[[Category: Tcell]] | [[Category: Tcell]] |
Revision as of 11:19, 24 December 2014
Crystal structure of a RNA binding domain of polyadenylate-binding protein (PABPN1) from Homo sapiens at 1.95 A resolution
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