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New page: left|200px<br /> <applet load="1ec6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ec6, resolution 2.40Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1ec6.gif|left|200px]]<br />
<applet load="1ec6" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ec6, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF NOVA-2 KH3 K-HOMOLOGY RNA-BINDING DOMAIN BOUND TO 20-MER RNA HAIRPIN'''<br />


==Overview==
==CRYSTAL STRUCTURE OF NOVA-2 KH3 K-HOMOLOGY RNA-BINDING DOMAIN BOUND TO 20-MER RNA HAIRPIN==
The structure of a Nova protein K homology (KH) domain recognizing, single-stranded RNA has been determined at 2.4 A resolution. Mammalian, Nova antigens (1 and 2) constitute an important family of regulators of, RNA metabolism in neurons, first identified using sera from cancer, patients with the autoimmune disorder paraneoplastic opsoclonus-myoclonus, ataxia (POMA). The structure of the third KH domain (KH3) of Nova-2 bound, to a stem loop RNA resembles a molecular vise, with 5'-Ura-Cyt-Ade-Cyt-3', pinioned between an invariant Gly-X-X-Gly motif and the variable loop., Tetranucleotide recognition is supported by an aliphatic alpha helix/beta, sheet RNA-binding platform, which mimics 5'-Ura-Gua-3' by making, Watson-Crick-like hydrogen bonds with 5'-Cyt-Ade-3'. Sequence conservation, suggests that fragile X mental retardation results from perturbation of, RNA binding by the FMR1 protein.
<StructureSection load='1ec6' size='340' side='right'caption='[[1ec6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ec6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EC6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=1ec6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ec6 OCA], [https://pdbe.org/1ec6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ec6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ec6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ec6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NOVA2_HUMAN NOVA2_HUMAN] May regulate RNA splicing or metabolism in a specific subset of developing neurons (By similarity). Binds single strand RNA.
== 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/ec/1ec6_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ec6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of a Nova protein K homology (KH) domain recognizing single-stranded RNA has been determined at 2.4 A resolution. Mammalian Nova antigens (1 and 2) constitute an important family of regulators of RNA metabolism in neurons, first identified using sera from cancer patients with the autoimmune disorder paraneoplastic opsoclonus-myoclonus ataxia (POMA). The structure of the third KH domain (KH3) of Nova-2 bound to a stem loop RNA resembles a molecular vise, with 5'-Ura-Cyt-Ade-Cyt-3' pinioned between an invariant Gly-X-X-Gly motif and the variable loop. Tetranucleotide recognition is supported by an aliphatic alpha helix/beta sheet RNA-binding platform, which mimics 5'-Ura-Gua-3' by making Watson-Crick-like hydrogen bonds with 5'-Cyt-Ade-3'. Sequence conservation suggests that fragile X mental retardation results from perturbation of RNA binding by the FMR1 protein.


==About this Structure==
Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome.,Lewis HA, Musunuru K, Jensen KB, Edo C, Chen H, Darnell RB, Burley SK Cell. 2000 Feb 4;100(3):323-32. PMID:10676814<ref>PMID:10676814</ref>
1EC6 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=1EC6 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome., Lewis HA, Musunuru K, Jensen KB, Edo C, Chen H, Darnell RB, Burley SK, Cell. 2000 Feb 4;100(3):323-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10676814 10676814]
</div>
<div class="pdbe-citations 1ec6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Chen, H.]]
[[Category: Chen H]]
[[Category: Edo, C.]]
[[Category: Edo C]]
[[Category: Jensen, K.B.]]
[[Category: Jensen KB]]
[[Category: Lewis, H.A.]]
[[Category: Lewis HA]]
[[Category: Musunuru, K.]]
[[Category: Musunuru K]]
[[Category: alpha-beta fold]]
[[Category: kh domain]]
[[Category: protein/rna structure]]
[[Category: rna-binding motif]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:42:03 2007''

Latest revision as of 03:44, 6 June 2025

CRYSTAL STRUCTURE OF NOVA-2 KH3 K-HOMOLOGY RNA-BINDING DOMAIN BOUND TO 20-MER RNA HAIRPIN

1ec6, resolution 2.40Å

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