1wf2: Difference between revisions

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[[Image:1wf2.gif|left|200px]]


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==Solution structure of RRM domain in HNRPC protein==
The line below this paragraph, containing "STRUCTURE_1wf2", creates the "Structure Box" on the page.
<StructureSection load='1wf2' size='340' side='right'caption='[[1wf2]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1wf2]] 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=1WF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WF2 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wf2 OCA], [https://pdbe.org/1wf2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wf2 RCSB], [https://www.ebi.ac.uk/pdbsum/1wf2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wf2 ProSAT], [https://www.topsan.org/Proteins/RSGI/1wf2 TOPSAN]</span></td></tr>
{{STRUCTURE_1wf2| PDB=1wf2 |  SCENE= }}
</table>
== 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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wf2 ConSurf].
<div style="clear:both"></div>


'''Solution structure of RRM domain in HNRPC protein'''
==See Also==
 
*[[Nucleoprotein 3D structures|Nucleoprotein 3D structures]]
 
== References ==
==About this Structure==
<references/>
1WF2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WF2 OCA].
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: He, F.]]
[[Category: He F]]
[[Category: Inoue, M.]]
[[Category: Inoue M]]
[[Category: Kigawa, T.]]
[[Category: Kigawa T]]
[[Category: Muto, Y.]]
[[Category: Muto Y]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Shirouzu M]]
[[Category: Shirouzu, M.]]
[[Category: Terada T]]
[[Category: Terada, T.]]
[[Category: Yokoyama S]]
[[Category: Yokoyama, S.]]
[[Category: Hnrpc protein]]
[[Category: Nmr]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: Rrm domain]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:33:55 2008''

Latest revision as of 16:36, 9 May 2024

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 Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
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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