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New page: left|200px<br /> <applet load="1dt4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dt4, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1dt4.gif|left|200px]]<br />
<applet load="1dt4" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dt4, resolution 2.6&Aring;" />
'''CRYSTAL STRUCTURE OF NOVA-1 KH3 K-HOMOLOGY RNA-BINDING DOMAIN'''<br />


==Overview==
==CRYSTAL STRUCTURE OF NOVA-1 KH3 K-HOMOLOGY RNA-BINDING DOMAIN==
BACKGROUND: Nova-1 and Nova-2 are related neuronal proteins that were, initially cloned using antisera obtained from patients with the autoimmune, neurological disease paraneoplastic opsoclonus-myoclonus ataxia (POMA)., Both of these disease gene products contain three RNA-binding motifs known, as K-homology or KH domains, and their RNA ligands have been identified, via binding-site selection experiments. The KH motif structure has been, determined previously using NMR spectroscopy, but not using X-ray, crystallography. Many proteins contain more than one KH domain, yet there, is no published structural information regarding the behavior of such, multimers. RESULTS: We have obtained the first X-ray crystallographic, structures of KH-domain-containing proteins. Structures of the third KH, domains (KH3) of Nova-1 and Nova-2 were determined by multiple isomorphous, replacement and molecular replacement at 2.6 A and 2.0 A, respectively., These highly similar RNA-binding motifs form a compact protease-resistant, domain resembling an open-faced sandwich, consisting of a three-stranded, antiparallel beta sheet topped by three alpha helices. In both Nova, crystals, the lattice is composed of symmetric tetramers of KH3 domains, that are created by two dimer interfaces. CONCLUSIONS: The crystal, structures of both Nova KH3 domains are similar to the previously, determined NMR structures. The most significant differences among the KH, domains involve changes in the positioning of one or more of the alpha, helices with respect to the betasheet, particularly in the NMR structure, of the KH1 domain of the Fragile X disease protein FMR-1. Loop regions in, the KH domains are clearly visible in the crystal structure, unlike the, NMR structures, revealing the conformation of the invariant Gly-X-X-Gly, segment that is thought to participate in RNA-binding and of the variable, region. The tetrameric arrangements of the Nova KH3 domains provide, insights into how KH domains may interact with each other in proteins, containing multiple KH motifs.
<StructureSection load='1dt4' size='340' side='right'caption='[[1dt4]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1dt4]] is a 1 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=1DT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DT4 FirstGlance]. <br>
1DT4 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=1DT4 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#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=1dt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dt4 OCA], [https://pdbe.org/1dt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dt4 RCSB], [https://www.ebi.ac.uk/pdbsum/1dt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dt4 ProSAT]</span></td></tr>
==Reference==
</table>
Crystal structures of Nova-1 and Nova-2 K-homology RNA-binding domains., Lewis HA, Chen H, Edo C, Buckanovich RJ, Yang YY, Musunuru K, Zhong R, Darnell RB, Burley SK, Structure. 1999 Feb 15;7(2):191-203. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10368286 10368286]
== Function ==
[https://www.uniprot.org/uniprot/NOVA1_HUMAN NOVA1_HUMAN] May regulate RNA splicing or metabolism in a specific subset of developing neurons.
== 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/dt/1dt4_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=1dt4 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Buckanovich, R.J.]]
[[Category: Buckanovich RJ]]
[[Category: Chen, H.]]
[[Category: Chen H]]
[[Category: Edo, C.]]
[[Category: Edo C]]
[[Category: Lewis, H.A.]]
[[Category: Lewis HA]]
[[Category: Yang, Y.Y.L.]]
[[Category: Yang YYL]]
[[Category: alpha-beta fold]]
[[Category: kh domain]]
[[Category: rna-binding motif]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:35:36 2007''

Latest revision as of 06:58, 7 February 2024

CRYSTAL STRUCTURE OF NOVA-1 KH3 K-HOMOLOGY RNA-BINDING DOMAIN

1dt4, resolution 2.60Å

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