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New page: left|200px<br /> <applet load="1go5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1go5" /> '''STRUCTURE OF THE C-TERMINAL FG-BINDING DOMA...
 
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[[Image:1go5.gif|left|200px]]<br />
<applet load="1go5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1go5" />
'''STRUCTURE OF THE C-TERMINAL FG-BINDING DOMAIN OF HUMAN TAP'''<br />


==Overview==
==Structure of the C-terminal FG-binding domain of human Tap==
The vertebrate Tap protein is a member of the NXF family of shuttling, transport receptors for nuclear export of mRNA. Tap has a modular, structure, and its most C-terminal domain is important for binding to FG, repeat-containing nuclear pore proteins (FG-nucleoporins) and is, sufficient to mediate nuclear shuttling. We report the solution structure, of this C-terminal domain, which is based on a distinctive arrangement of, four alpha-helices and is joined to the next module by a flexible, 12-residue Pro-rich linker. F617A Tap suppresses FG-nucleoporin binding by, the most C-terminal domain that, together with the structure of the other, modules from which Tap is constructed, provides a structural context for, its nuclear shuttling function.
<StructureSection load='1go5' size='340' side='right'caption='[[1go5]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1go5]] 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=1GO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GO5 FirstGlance]. <br>
</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=1go5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1go5 OCA], [https://pdbe.org/1go5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1go5 RCSB], [https://www.ebi.ac.uk/pdbsum/1go5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1go5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NXF1_HUMAN NXF1_HUMAN] Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm. The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5.<ref>PMID:9660949</ref> <ref>PMID:19165146</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/go/1go5_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=1go5 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The vertebrate Tap protein is a member of the NXF family of shuttling transport receptors for nuclear export of mRNA. Tap has a modular structure, and its most C-terminal domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling. We report the solution structure of this C-terminal domain, which is based on a distinctive arrangement of four alpha-helices and is joined to the next module by a flexible 12-residue Pro-rich linker. F617A Tap suppresses FG-nucleoporin binding by the most C-terminal domain that, together with the structure of the other modules from which Tap is constructed, provides a structural context for its nuclear shuttling function.


==Disease==
Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1.,Grant RP, Hurt E, Neuhaus D, Stewart M Nat Struct Biol. 2002 Apr;9(4):247-51. PMID:11875519<ref>PMID:11875519</ref>
Known diseases associated with this structure: Bare lymphocyte syndrome, type I OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=170260 170260]]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1GO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GO5 OCA].
</div>
 
<div class="pdbe-citations 1go5" style="background-color:#fffaf0;"></div>
==Reference==
== References ==
Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1., Grant RP, Hurt E, Neuhaus D, Stewart M, Nat Struct Biol. 2002 Apr;9(4):247-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11875519 11875519]
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Grant, R.P.]]
[[Category: Grant RP]]
[[Category: Hurt, E.]]
[[Category: Hurt E]]
[[Category: Neuhaus, D.]]
[[Category: Neuhaus D]]
[[Category: Stewart, M.]]
[[Category: Stewart M]]
[[Category: mrna export]]
[[Category: nuclear transport]]
[[Category: nucleoporins]]
[[Category: uba]]
 
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