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PDBsum entry 2sxl
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RNA-binding domain
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PDB id
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2sxl
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References listed in PDB file
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Key reference
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Title
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A characteristic arrangement of aromatic amino acid residues in the solution structure of the amino-Terminal RNA-Binding domain of drosophila sex-Lethal.
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Authors
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M.Inoue,
Y.Muto,
H.Sakamoto,
T.Kigawa,
K.Takio,
Y.Shimura,
S.Yokoyama.
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Ref.
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J Mol Biol, 1997,
272,
82-94.
[DOI no: ]
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PubMed id
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Abstract
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The Sex-lethal (Sxl) protein from Drosophila melanogaster has two RNA-binding
domains (RBDs). As the amino-terminal RBD (RBD1) of the Sxl protein exhibits low
sequence homology to the typical RBDs, particularly at the putative functional
residues, it was difficult to unambiguously locate the RNP1 and RNP2 motifs.
Therefore, in the present study, we defined the amino and carboxy-terminal
borders of the first RNA-binding domain (RBD1) of the Sxl protein by limited
tryptic digestion. By replacement of Phe166 by Tyr, we constructed a highly
soluble mutant, which exhibits the same RNA-binding properties as those of the
wild-type. Using this mutant protein, we performed NMR measurements, and
elucidated the secondary and tertiary structures of the Sxl RBD1 in solution.
The betaalphabetabetaalphabeta folding pattern is conserved in the solution
structure of the Sxl RBD1, as in other reported RBD structures. This allowed us
to identify both the RNP1 and RNP2 motifs of the Sxl RBD1 unambiguously.
Intriguingly, the RNP2 motif of the Sxl RBD1 has an Ile residue at the second
position, which is generally occupied by an aromatic amino acid residue in RBDs
and has been suggested to be involved in their RNA binding. Furthermore, the
loop region between beta2 and beta3 of the Sxl RBD1 has an exceptional cluster
of aromatic amino acid residues, in place of the normal basic amino acid
cluster. In contrast, the second RBD of Sxl does not exhibit these
characteristic features.
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Figure 2.
Figure 2. Schematic representation of the Sxl fragments.
The numbering corresponds to the full-length Sxl protein. The
putative trypsin-cleavable sites are indicated as vertical lines
on LRBD1-2. The major cleavage sites are indicated with
triangles.
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Figure 12.
Figure 12. Amino acid types (%) in the RNP2 (a) and β2/β3
loop-RNP1 (b) regions of 161 RBDs homologous to either RBD1 or
RBD2. Amino acid categorization: aliphatic (A, V, L, I, and M),
aromatic (F, Y, and W), basic (K and R), acidic (D and E),
neutral (S, T, C, N, Q, and H), and small (G and P).
Non-consensus amino acid residues of RBD1 are shown in white
letters on black disks. The highest percentage for each residue
is indicated in bold letters.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1997,
272,
82-94)
copyright 1997.
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Secondary reference #1
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Title
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Crystal structure at 1.92 a resolution of the RNA-Binding domain of the u1a spliceosomal protein complexed with an RNA hairpin.
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Authors
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C.Oubridge,
N.Ito,
P.R.Evans,
C.H.Teo,
K.Nagai.
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Ref.
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Nature, 1994,
372,
432-438.
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PubMed id
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Secondary reference #2
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Title
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Resonance assignments and solution structure of the second RNA-Binding domain of sex-Lethal determined by multidimensional heteronuclear magnetic resonance.
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Authors
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A.L.Lee,
R.Kanaar,
D.C.Rio,
D.E.Wemmer.
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Ref.
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Biochemistry, 1994,
33,
13775-13786.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Determination of the secondary structure and folding topology of an RNA binding domain of mammalian hnrnp a1 protein using three-Dimensional heteronuclear magnetic resonance spectroscopy.
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Authors
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D.S.Garrett,
P.J.Lodi,
Y.Shamoo,
K.R.Williams,
G.M.Clore,
A.M.Gronenborn.
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Ref.
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Biochemistry, 1994,
33,
2852-2858.
[DOI no: ]
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PubMed id
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Secondary reference #4
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Title
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1h, 13c, And 15n nmr assignments and global folding pattern of the RNA-Binding domain of the human hnrnp c proteins.
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Authors
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M.Wittekind,
M.Görlach,
M.Friedrichs,
G.Dreyfuss,
L.Mueller.
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Ref.
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Biochemistry, 1992,
31,
6254-6265.
[DOI no: ]
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PubMed id
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Secondary reference #5
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Title
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Crystal structure of the RNA-Binding domain of the u1 small nuclear ribonucleoprotein a.
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Authors
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K.Nagai,
C.Oubridge,
T.H.Jessen,
J.Li,
P.R.Evans.
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Ref.
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Nature, 1990,
348,
515-520.
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PubMed id
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