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PDBsum entry 1m9o
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Metal binding protein
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PDB id
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1m9o
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
42:217-221
(2003)
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PubMed id:
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A Cys3His zinc-binding domain from Nup475/tristetraprolin: a novel fold with a disklike structure.
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B.T.Amann,
M.T.Worthington,
J.M.Berg.
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ABSTRACT
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Nup475 (also known as tristetraprolin and TIS11) includes two zinc-binding
domains of the form Cys-X8-Cys-X5-Cys-X3-His. These domains are required for
rapid degradation of tumor necrosis factor (TNF) and other mRNAs through the
interaction with AU-rich elements in their 3'-untranslated regions. The
three-dimensional solution structure of the first domain was determined by
multidimensional nuclear magnetic resonance spectroscopy, revealing a novel fold
around a central zinc ion. The core structure is disk-like with a diameter of
approximately 25 A and a width of approximately 12 A. This structure provides a
basis for evaluating the role of individual residues for structural stability
and for nucleic acid binding.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.S.Boukhvalova,
G.A.Prince,
and
J.C.Blanco
(2010).
Inactivation of respiratory syncytial virus by zinc finger reactive compounds.
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Virol J,
7,
20.
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M.Baou,
A.Jewell,
and
J.J.Murphy
(2009).
TIS11 family proteins and their roles in posttranscriptional gene regulation.
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J Biomed Biotechnol,
2009,
634520.
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R.M.Rowlett,
C.A.Chrestensen,
M.J.Schroeder,
M.G.Harp,
J.W.Pelo,
J.Shabanowitz,
R.DeRose,
D.F.Hunt,
T.W.Sturgill,
and
M.T.Worthington
(2008).
Inhibition of tristetraprolin deadenylation by poly(A) binding protein.
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Am J Physiol Gastrointest Liver Physiol,
295,
G421-G430.
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J.A.Vila,
M.E.Villegas,
H.A.Baldoni,
and
H.A.Scheraga
(2007).
Predicting 13Calpha chemical shifts for validation of protein structures.
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J Biomol NMR,
38,
221-235.
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M.Saravanan,
K.Vasu,
S.Ghosh,
and
V.Nagaraja
(2007).
Dual role for Zn2+ in maintaining structural integrity and inducing DNA sequence specificity in a promiscuous endonuclease.
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J Biol Chem,
282,
32320-32326.
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B.Y.Brewer,
J.D.Ballin,
E.J.Fialcowitz-White,
P.J.Blackshear,
and
G.M.Wilson
(2006).
Substrate dependence of conformational changes in the RNA-binding domain of tristetraprolin assessed by fluorescence spectroscopy of tryptophan mutants.
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Biochemistry,
45,
13807-13817.
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B.P.Hudson,
M.A.Martinez-Yamout,
H.J.Dyson,
and
P.E.Wright
(2004).
Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d.
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Nat Struct Mol Biol,
11,
257-264.
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PDB code:
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C.A.Chrestensen,
M.J.Schroeder,
J.Shabanowitz,
D.F.Hunt,
J.W.Pelo,
M.T.Worthington,
and
T.W.Sturgill
(2004).
MAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sites including Ser178, a site required for 14-3-3 binding.
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J Biol Chem,
279,
10176-10184.
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H.Cao
(2004).
Expression, purification, and biochemical characterization of the antiinflammatory tristetraprolin: a zinc-dependent mRNA binding protein affected by posttranslational modifications.
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Biochemistry,
43,
13724-13738.
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C.R.Cook,
G.Kung,
F.C.Peterson,
B.F.Volkman,
and
M.Lei
(2003).
A novel zinc finger is required for Mcm10 homocomplex assembly.
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J Biol Chem,
278,
36051-36058.
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P.J.Blackshear,
W.S.Lai,
E.A.Kennington,
G.Brewer,
G.M.Wilson,
X.Guan,
and
P.Zhou
(2003).
Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates.
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J Biol Chem,
278,
19947-19955.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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