 |
PDBsum entry 1ec6
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
RNA binding protein/RNA
|
PDB id
|
|
|
|
1ec6
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Sequence-Specific RNA binding by a nova kh domain: implications for paraneoplastic disease and the fragile X syndrome.
|
|
|
Authors
|
|
H.A.Lewis,
K.Musunuru,
K.B.Jensen,
C.Edo,
H.Chen,
R.B.Darnell,
S.K.Burley.
|
|
|
Ref.
|
|
Cell, 2000,
100,
323-332.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|
|
|
|
|
Figure 2.
Figure 2. Stem Loop RNA StructuresSchematic drawings of the
stem loop crystallization RNAs in complexes 1 and 2. Nucleotides
making direct protein contacts are denoted with *. Color coding
denotes nucleotides making extensive protein contacts (Ade-11
through Cyt-15; magenta, pink, gold, green, and blue) and the
remaining nucleotides (gray).
|
|
Figure 5.
Figure 5. 5′-Ura-Cyt-Ade-Cyt-3′ Binding by Nova-2
KH3RIBBONS drawings showing the RNA-binding surface sandwiched
between the invariant Gly-X-X-Gly motif (yellow) and the
variable loop (red). The portion of the stem loop
crystallization RNA making extensive protein contacts has been
included as a color-coded stick figure (Figure 2) with the
aliphatic residues (gray) comprising the hydrophobic α/β RNA
binding platform. (A) shows the entire complex. (B), (C), and
(D) show the environments of Ade-11 Ura-12, and Cyt-13,
respectively. (E) shows the environments of Ade-14 and Cyt-15.
The side chain of Leu-28 is denoted with *. (F) corresponds to
the views used in (D) and (E), with the overlying RNA removed,
and shows the aliphatic platform with the jaws of the molecular
vise.
|
|
|
|
|
|
The above figures are
reprinted
by permission from Cell Press:
Cell
(2000,
100,
323-332)
copyright 2000.
|
|
|
|
|
|
|
