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

<StructureSection load='1ec6' size='340' side='right'caption='[[1ec6]], [[Resolution|resolution]] 2.40&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ec6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EC6 FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ec6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ec6 OCA], [http://pdbe.org/1ec6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ec6 RCSB], [http://www.ebi.ac.uk/pdbsum/1ec6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ec6 ProSAT]</span></td></tr>

== Function ==

[[http://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.

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== 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.

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>

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

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<div class="pdbe-citations 1ec6" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Chen, H]]

[[Category: Alpha-beta fold]]

[[Category: Rna-binding motif]]