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PDBsum entry 2anr
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RNA-binding protein/RNA
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PDB id
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2anr
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Contents |
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* Residue conservation analysis
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PDB id:
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RNA-binding protein/RNA
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Title:
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Crystal structure (ii) of nova-1 kh1/kh2 domain tandem with 25nt RNA hairpin
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Structure:
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5'-r( Cp (5Bu) p Cp Gp Cp Gp Gp Ap Up Cp Ap Gp Up Cp Ap Cp Cp Cp Ap Ap Gp Cp Gp Ap G )-3'. Chain: b. Engineered: yes. RNA-binding protein nova-1. Chain: a. Fragment: kh1/kh2 domains. Synonym: neuro-oncological ventral antigen 1,ventral neuron-specific
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Source:
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Synthetic: yes. Mus musculus. Mouse. Organism_taxid: 10090. Gene: nova1. Expressed in: escherichia coli. Expression_system_taxid: 562
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Biol. unit:
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Dimer (from
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Resolution:
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1.94Å
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R-factor:
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0.230
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R-free:
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0.268
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Authors:
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L.Malinina,M.Teplova,K.Musunuru,A.Teplov,J.C.Darnell,S.K.Burley, R.B.Darnell,D.J.Patel
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Key ref:
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M.Teplova
et al.
(2011).
Protein-RNA and protein-protein recognition by dual KH1/2 domains of the neuronal splicing factor Nova-1.
Structure,
19,
930-944.
PubMed id:
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Date:
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11-Aug-05
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Release date:
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24-Oct-06
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PROCHECK
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Headers
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References
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P51513
(NOVA1_HUMAN) -
RNA-binding protein Nova-1 from Homo sapiens
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Seq:
Struc:
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507 a.a.
155 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 5 residue positions (black
crosses)
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C-5BU-C-G-C-G-G-A-U-C-A-G-U-C-A-C-C-C-A-A-G-C-G-A-G
25 bases
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Structure
19:930-944
(2011)
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PubMed id:
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Protein-RNA and protein-protein recognition by dual KH1/2 domains of the neuronal splicing factor Nova-1.
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M.Teplova,
L.Malinina,
J.C.Darnell,
J.Song,
M.Lu,
R.Abagyan,
K.Musunuru,
A.Teplov,
S.K.Burley,
R.B.Darnell,
D.J.Patel.
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ABSTRACT
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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.
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Links
