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| | ==Solution structure of a C terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB)== | | ==Solution structure of a C terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB)== |
| - | <StructureSection load='2mju' size='340' side='right' caption='[[2mju]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2mju' size='340' side='right'caption='[[2mju]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mju]] 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=2MJU OCA]. <br> | + | <table><tr><td colspan='2'>[[2mju]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MJU FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTBP2, NPTB, PTB, PTBLP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </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=2mju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mju OCA], [https://pdbe.org/2mju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mju RCSB], [https://www.ebi.ac.uk/pdbsum/2mju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mju ProSAT]</span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mju OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mju RCSB], [http://www.ebi.ac.uk/pdbsum/2mju PDBsum]</span></td></tr> | + | </table> |
| - | <table> | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PTBP2_HUMAN PTBP2_HUMAN] RNA-binding protein which binds to intronic polypyrimidine tracts and mediates negative regulation of exons splicing. May antagonize in a tissue-specific manner the ability of NOVA1 to activate exon selection. Beside its function in pre-mRNA splicing, plays also a role in the regulation of translation. Isoform 5 has a reduced affinity for RNA.<ref>PMID:11003644</ref> <ref>PMID:12667457</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | Solution and crystal structures of a C-terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB).,Joshi A, Esteve V, Buckroyd AN, Blatter M, Allain FH, Curry S PeerJ. 2014 Mar 13;2:e305. doi: 10.7717/peerj.305. eCollection 2014. PMID:24688880<ref>PMID:24688880</ref> | | Solution and crystal structures of a C-terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB).,Joshi A, Esteve V, Buckroyd AN, Blatter M, Allain FH, Curry S PeerJ. 2014 Mar 13;2:e305. doi: 10.7717/peerj.305. eCollection 2014. PMID:24688880<ref>PMID:24688880</ref> |
| | | | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2mju" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Allain, F H.T.]] | + | [[Category: Large Structures]] |
| - | [[Category: Blatter, M.]] | + | [[Category: Allain FH-T]] |
| - | [[Category: Esteve, V.]] | + | [[Category: Blatter M]] |
| - | [[Category: Nptb]] | + | [[Category: Esteve V]] |
| - | [[Category: Splicing]]
| + | |
| Structural highlights
Function
PTBP2_HUMAN RNA-binding protein which binds to intronic polypyrimidine tracts and mediates negative regulation of exons splicing. May antagonize in a tissue-specific manner the ability of NOVA1 to activate exon selection. Beside its function in pre-mRNA splicing, plays also a role in the regulation of translation. Isoform 5 has a reduced affinity for RNA.[1] [2]
Publication Abstract from PubMed
The eukaryotic polypyrimidine tract binding protein (PTB) serves primarily as a regulator of alternative splicing of messenger RNA, but is also co-opted to other roles such as RNA localisation and translation initiation from internal ribosome entry sites. The neuronal paralogue of PTB (nPTB) is 75% identical in amino acid sequence with PTB. Although the two proteins have broadly similar RNA binding specificities and effects on RNA splicing, differential expression of PTB and nPTB can lead to the generation of alternatively spliced mRNAs. RNA binding by PTB and nPTB is mediated by four RNA recognition motifs (RRMs). We present here the crystal and solution structures of the C-terminal domain of nPTB (nPTB34) which contains RRMs 3 and 4. As expected the structures are similar to each other and to the solution structure of the equivalent fragment from PTB (PTB34). The result confirms that, as found for PTB, RRMs 3 and 4 of nPTB interact with one another to form a stable unit that presents the RNA-binding surfaces of the component RRMs on opposite sides that face away from each other. The major differences between PTB34 and nPTB34 arise from amino acid side chain substitutions on the exposed beta-sheet surfaces and adjoining loops of each RRM, which are likely to modulate interactions with RNA.
Solution and crystal structures of a C-terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB).,Joshi A, Esteve V, Buckroyd AN, Blatter M, Allain FH, Curry S PeerJ. 2014 Mar 13;2:e305. doi: 10.7717/peerj.305. eCollection 2014. PMID:24688880[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Markovtsov V, Nikolic JM, Goldman JA, Turck CW, Chou MY, Black DL. Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein. Mol Cell Biol. 2000 Oct;20(20):7463-79. PMID:11003644
- ↑ Mitchell SA, Spriggs KA, Coldwell MJ, Jackson RJ, Willis AE. The Apaf-1 internal ribosome entry segment attains the correct structural conformation for function via interactions with PTB and unr. Mol Cell. 2003 Mar;11(3):757-71. PMID:12667457
- ↑ Joshi A, Esteve V, Buckroyd AN, Blatter M, Allain FH, Curry S. Solution and crystal structures of a C-terminal fragment of the neuronal isoform of the polypyrimidine tract binding protein (nPTB). PeerJ. 2014 Mar 13;2:e305. doi: 10.7717/peerj.305. eCollection 2014. PMID:24688880 doi:http://dx.doi.org/10.7717/peerj.305
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