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| | <StructureSection load='3b4d' size='340' side='right'caption='[[3b4d]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3b4d' size='340' side='right'caption='[[3b4d]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3b4d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B4D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3b4d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B4D FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3b4m|3b4m]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.001Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PABPN1, PAB2, PABP2 ([https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3b4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b4d OCA], [https://pdbe.org/3b4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b4d RCSB], [https://www.ebi.ac.uk/pdbsum/3b4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b4d ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b4d OCA], [https://pdbe.org/3b4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b4d RCSB], [https://www.ebi.ac.uk/pdbsum/3b4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b4d ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/PABP2_HUMAN PABP2_HUMAN]] Defects in PABPN1 are the cause of oculopharyngeal muscular dystrophy (OPMD) [MIM:[https://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>
| + | [https://www.uniprot.org/uniprot/PABP2_HUMAN PABP2_HUMAN] Defects in PABPN1 are the cause of oculopharyngeal muscular dystrophy (OPMD) [MIM:[https://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 == | | == Function == |
| - | [[https://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>
| + | [https://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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ge, H]] | + | [[Category: Ge H]] |
| - | [[Category: Niu, L]] | + | [[Category: Niu L]] |
| - | [[Category: Teng, M]] | + | [[Category: Teng M]] |
| - | [[Category: Tong, S]] | + | [[Category: Tong S]] |
| - | [[Category: Acetylation]]
| + | |
| - | [[Category: Alpha-beta sandwich structure]]
| + | |
| - | [[Category: Alternative splicing]]
| + | |
| - | [[Category: Coiled coil]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Disease mutation]]
| + | |
| - | [[Category: Methylation]]
| + | |
| - | [[Category: Mrna processing]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| - | [[Category: Rna binding domain]]
| + | |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Rna recognition motif]]
| + | |
| - | [[Category: Rna-binding]]
| + | |
| - | [[Category: Rrm fold]]
| + | |
| - | [[Category: Triplet repeat expansion]]
| + | |
| Structural highlights
Disease
PABP2_HUMAN Defects in PABPN1 are the cause of oculopharyngeal muscular dystrophy (OPMD) [MIM: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.[1] [2]
Function
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).[3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Brais B, Bouchard JP, Xie YG, Rochefort DL, Chretien N, Tome FM, Lafreniere RG, Rommens JM, Uyama E, Nohira O, Blumen S, Korczyn AD, Heutink P, Mathieu J, Duranceau A, Codere F, Fardeau M, Rouleau GA. Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy. Nat Genet. 1998 Feb;18(2):164-7. PMID:9462747 doi:10.1038/ng0298-164
- ↑ van der Sluijs BM, van Engelen BG, Hoefsloot LH. Oculopharyngeal muscular dystrophy (OPMD) due to a small duplication in the PABPN1 gene. Hum Mutat. 2003 May;21(5):553. PMID:12673802 doi:10.1002/humu.9138
- ↑ Fan X, Dion P, Laganiere J, Brais B, Rouleau GA. Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death. Hum Mol Genet. 2001 Oct 1;10(21):2341-51. PMID:11689481
- ↑ Kim YJ, Noguchi S, Hayashi YK, Tsukahara T, Shimizu T, Arahata K. The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression. Hum Mol Genet. 2001 May 15;10(11):1129-39. PMID:11371506
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