==Crystal structure (II) of Nova-1 KH1/KH2 domain tandem with 25nt RNA hairpin==

<StructureSection load='2anr' size='340' side='right'caption='[[2anr]], [[Resolution|resolution]] 1.94&Aring;' scene=''>

<table><tr><td colspan='2'>[[2anr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ANR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ANR FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2anr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2anr OCA], [https://pdbe.org/2anr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2anr RCSB], [https://www.ebi.ac.uk/pdbsum/2anr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2anr ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/NOVA1_HUMAN NOVA1_HUMAN]] May regulate RNA splicing or metabolism in a specific subset of developing neurons.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Nova onconeural antigens are neuron-specific RNA-binding proteins implicated in paraneoplastic opsoclonus-myoclonus-ataxia (POMA) syndrome. Nova harbors three K-homology (KH) motifs implicated in alternate splicing regulation of genes involved in inhibitory synaptic transmission. We report the crystal structure of the first two KH domains (KH1/2) of Nova-1 bound to an in vitro selected RNA hairpin, containing a UCAG-UCAC high-affinity binding site. Sequence-specific intermolecular contacts in the complex involve KH1 and the second UCAC repeat, with the RNA scaffold buttressed by interactions between repeats. Whereas the canonical RNA-binding surface of KH2 in the above complex engages in protein-protein interactions in the crystalline state, the individual KH2 domain can sequence-specifically target the UCAC RNA element in solution. The observed antiparallel alignment of KH1 and KH2 domains in the crystal structure of the complex generates a scaffold that could facilitate target pre-mRNA looping on Nova binding, thereby potentially explaining Nova's functional role in splicing regulation.

Protein-RNA and protein-protein recognition by dual KH1/2 domains of the neuronal splicing factor Nova-1.,Teplova M, Malinina L, Darnell JC, Song J, Lu M, Abagyan R, Musunuru K, Teplov A, Burley SK, Darnell RB, Patel DJ Structure. 2011 Jul 13;19(7):930-44. PMID:21742260<ref>PMID:21742260</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2anr" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Burley, S K]]

[[Category: Protein-rna complex]]

[[Category: Rna-binding protein-rna complex]]