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| | ==Solution structure of hnRNP C RRM in complex with 5'-UUUUC-3' RNA== | | ==Solution structure of hnRNP C RRM in complex with 5'-UUUUC-3' RNA== |
| - | <StructureSection load='2mz1' size='340' side='right'caption='[[2mz1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2mz1' size='340' side='right'caption='[[2mz1]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mz1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MZ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mz1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MZ1 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HNRNPC, HNRPC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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=2mz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mz1 OCA], [https://pdbe.org/2mz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mz1 RCSB], [https://www.ebi.ac.uk/pdbsum/2mz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mz1 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=2mz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mz1 OCA], [https://pdbe.org/2mz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mz1 RCSB], [https://www.ebi.ac.uk/pdbsum/2mz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mz1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/HNRPC_HUMAN HNRPC_HUMAN]] Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.<ref>PMID:8264621</ref> <ref>PMID:7567451</ref> <ref>PMID:12509468</ref> <ref>PMID:16010978</ref>
| + | [https://www.uniprot.org/uniprot/HNRPC_HUMAN HNRPC_HUMAN] Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.<ref>PMID:8264621</ref> <ref>PMID:7567451</ref> <ref>PMID:12509468</ref> <ref>PMID:16010978</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: Allain, F H.T]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Cienikova, Z]] | + | [[Category: Allain FH-T]] |
| - | [[Category: Damberger, F F]] | + | [[Category: Cienikova Z]] |
| - | [[Category: Hall, J]] | + | [[Category: Damberger FF]] |
| - | [[Category: Maris, C]] | + | [[Category: Hall J]] |
| - | [[Category: Complex]]
| + | [[Category: Maris C]] |
| - | [[Category: Hnrnp c]]
| + | |
| - | [[Category: Rna binding protein-rna complex]]
| + | |
| - | [[Category: Rrm]]
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| Structural highlights
Function
HNRPC_HUMAN Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules.[1] [2] [3] [4]
Publication Abstract from PubMed
HnRNP C is a ubiquitous RNA regulatory factor and the principal constituent of the nuclear hnRNP core particle. The protein contains one amino-terminal RNA recognition motif (RRM) known to bind uridine (U)-rich sequences. This work provides a molecular and mechanistic understanding of this interaction. We solved the solution structures of the RRM in complex with poly(U) oligomers of five and seven nucleotides. The five binding pockets of RRM recognize uridines with an unusual 5'-to-3' gradient of base selectivity. The target recognition is therefore strongly sensitive to base clustering, explaining the preference for contiguous uridine tracts. Using a novel approach integrating the structurally derived recognition consensus of the RRM with a thermodynamic description of its multi-register binding, we modeled the saturation of cellular uridine tracts by this protein. The binding pattern is remarkably consistent with the experimentally observed transcriptome-wide cross-link distribution of the full-length hnRNP C on short uridine tracts. This result re-establishes the RRM as the primary RNA-binding domain of the hnRNP C tetramer and provides a proof of concept for interpreting high-throughput interaction data using structural approaches.
Structural and mechanistic insights into poly(uridine) tract recognition by the hnRNP C RNA recognition motif.,Cienikova Z, Damberger FF, Hall J, Allain FH, Maris C J Am Chem Soc. 2014 Oct 15;136(41):14536-44. doi: 10.1021/ja507690d. Epub 2014, Sep 30. PMID:25216038[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huang M, Rech JE, Northington SJ, Flicker PF, Mayeda A, Krainer AR, LeStourgeon WM. The C-protein tetramer binds 230 to 240 nucleotides of pre-mRNA and nucleates the assembly of 40S heterogeneous nuclear ribonucleoprotein particles. Mol Cell Biol. 1994 Jan;14(1):518-33. PMID:8264621
- ↑ Sebillon P, Beldjord C, Kaplan JC, Brody E, Marie J. A T to G mutation in the polypyrimidine tract of the second intron of the human beta-globin gene reduces in vitro splicing efficiency: evidence for an increased hnRNP C interaction. Nucleic Acids Res. 1995 Sep 11;23(17):3419-25. PMID:7567451
- ↑ Kim JH, Paek KY, Choi K, Kim TD, Hahm B, Kim KT, Jang SK. Heterogeneous nuclear ribonucleoprotein C modulates translation of c-myc mRNA in a cell cycle phase-dependent manner. Mol Cell Biol. 2003 Jan;23(2):708-20. PMID:12509468
- ↑ Shetty S. Regulation of urokinase receptor mRNA stability by hnRNP C in lung epithelial cells. Mol Cell Biochem. 2005 Apr;272(1-2):107-18. PMID:16010978
- ↑ Cienikova Z, Damberger FF, Hall J, Allain FH, Maris C. Structural and mechanistic insights into poly(uridine) tract recognition by the hnRNP C RNA recognition motif. J Am Chem Soc. 2014 Oct 15;136(41):14536-44. doi: 10.1021/ja507690d. Epub 2014, Sep 30. PMID:25216038 doi:http://dx.doi.org/10.1021/ja507690d
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