2mz1: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<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>
<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='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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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>  
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== 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<ref>PMID:25216038</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mz1" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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Retrieved from "https://proteopedia.org/2mz1"