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| | <StructureSection load='3zzz' size='340' side='right'caption='[[3zzz]], [[Resolution|resolution]] 1.55Å' scene=''> | | <StructureSection load='3zzz' size='340' side='right'caption='[[3zzz]], [[Resolution|resolution]] 1.55Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zzz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZZZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zzz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZZZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZZZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></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]] 1.55Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qm9|1qm9]], [[1sjr|1sjr]], [[2adb|2adb]], [[2ad9|2ad9]], [[2adc|2adc]], [[2evz|2evz]], [[1sjq|1sjq]], [[1wi6|1wi6]], [[3zzy|3zzy]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></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=3zzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zzz OCA], [https://pdbe.org/3zzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zzz RCSB], [https://www.ebi.ac.uk/pdbsum/3zzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zzz 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=3zzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zzz OCA], [https://pdbe.org/3zzz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zzz RCSB], [https://www.ebi.ac.uk/pdbsum/3zzz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zzz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PTBP1_HUMAN PTBP1_HUMAN]] Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10.<ref>PMID:11003644</ref> <ref>PMID:15009664</ref> <ref>PMID:16260624</ref> <ref>PMID:21518792</ref> <ref>PMID:16179478</ref> [[https://www.uniprot.org/uniprot/RAVR1_MOUSE RAVR1_MOUSE]] Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA.<ref>PMID:14633994</ref>
| + | [https://www.uniprot.org/uniprot/RAVR1_MOUSE RAVR1_MOUSE] Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA.<ref>PMID:14633994</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Curry, S]] | + | [[Category: Curry S]] |
| - | [[Category: Joshi, A]] | + | [[Category: Joshi A]] |
| - | [[Category: Kotik-Kogan, O]] | + | [[Category: Kotik-Kogan O]] |
| - | [[Category: Peptide binding]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Rna recognition motif]]
| + | |
| Structural highlights
Function
RAVR1_MOUSE Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA.[1]
Publication Abstract from PubMed
The polypyrimidine tract-binding protein (PTB) is an important regulator of alternative splicing. PTB-regulated splicing of alpha-tropomyosin is enhanced by Raver1, a protein with four PTB-Raver1 interacting motifs (PRIs) that bind to the helical face of the second RNA recognition motif (RRM2) in PTB. We present the crystal structures of RRM2 in complex with PRI3 and PRI4 from Raver1, which-along with structure-based mutagenesis-reveal the molecular basis of their differential binding. High-affinity binding by Raver1 PRI3 involves shape-matched apolar contacts complemented by specific hydrogen bonds, a new variant of an established mode of peptide-RRM interaction. Our results refine the sequence of the PRI motif and place important structural constraints on functional models of PTB-Raver1 interactions. Our analysis indicates that the observed Raver1-PTB interaction is a general mode of binding that applies to Raver1 complexes with PTB paralogues such as nPTB and to complexes of Raver2 with PTB.
Crystallographic analysis of polypyrimidine tract-binding protein-raver1 interactions involved in regulation of alternative splicing.,Joshi A, Coelho MB, Kotik-Kogan O, Simpson PJ, Matthews SJ, Smith CW, Curry S Structure. 2011 Dec 7;19(12):1816-25. PMID:22153504[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gromak N, Rideau A, Southby J, Scadden AD, Gooding C, Huttelmaier S, Singer RH, Smith CW. The PTB interacting protein raver1 regulates alpha-tropomyosin alternative splicing. EMBO J. 2003 Dec 1;22(23):6356-64. PMID:14633994 doi:http://dx.doi.org/10.1093/emboj/cdg609
- ↑ Joshi A, Coelho MB, Kotik-Kogan O, Simpson PJ, Matthews SJ, Smith CW, Curry S. Crystallographic analysis of polypyrimidine tract-binding protein-raver1 interactions involved in regulation of alternative splicing. Structure. 2011 Dec 7;19(12):1816-25. PMID:22153504 doi:10.1016/j.str.2011.09.020
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