1wf2: Difference between revisions

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==Solution structure of RRM domain in HNRPC protein==
==Solution structure of RRM domain in HNRPC protein==
<StructureSection load='1wf2' size='340' side='right' caption='[[1wf2]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1wf2' size='340' side='right' caption='[[1wf2]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<table><tr><td colspan='2'>[[1wf2]] 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=1WF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WF2 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1wf2]] 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=1WF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WF2 FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">adKA0528 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">adKA0528 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wf2 OCA], [http://pdbe.org/1wf2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wf2 RCSB], [http://www.ebi.ac.uk/pdbsum/1wf2 PDBsum], [http://www.topsan.org/Proteins/RSGI/1wf2 TOPSAN]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wf2 OCA], [http://pdbe.org/1wf2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wf2 RCSB], [http://www.ebi.ac.uk/pdbsum/1wf2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wf2 ProSAT], [http://www.topsan.org/Proteins/RSGI/1wf2 TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wf/1wf2_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wf/1wf2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 19:33, 11 April 2018

Solution structure of RRM domain in HNRPC proteinSolution structure of RRM domain in HNRPC protein

Structural highlights

1wf2 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:adKA0528 (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
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