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PDBsum entry 1g2s
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* Residue conservation analysis
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DOI no:
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Biochemistry
40:7820-7831
(2001)
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PubMed id:
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NMR solution structure and backbone dynamics of the CC chemokine eotaxin-3.
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J.Ye,
K.L.Mayer,
M.R.Mayer,
M.J.Stone.
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ABSTRACT
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Eotaxin-3 is one of three related chemokines that specifically activate
chemokine receptor CCR3. We report the 3D structure and backbone dynamics of
eotaxin-3 determined by NMR spectroscopy. Eotaxin-3 is monomeric under the
conditions in this study and consists of an unstructured N-terminus before the
first two conserved cysteine residues, an irregularly structured N-loop
following the second conserved cysteine, a single turn of 3(10)-helix, a
three-stranded antiparallel beta-sheet, an alpha-helix, and an unstructured
C-terminal tail. As in other chemokines, the alpha-helix packs against one face
of the beta-sheet. The average backbone and heavy atom rmsd values of the 20
structures (residues 9-65) are 0.44 and 1.01 A, respectively. A comparison
between the structures of eotaxin-3 and related chemokines suggests that the
electrostatic potential in the vicinity of a surface groove and the structure of
the beta2-beta3 turn may be important for maintaining receptor specificity. The
backbone dynamics of eotaxin-3 were determined from 15N NMR relaxation data
using the extended model free dynamics formalism. Large amplitude motions on the
picosecond to nanosecond time scale were observed in both termini and in some
residues in the N-loop, the beta1-beta2 turn, and the beta3 strand; the location
of these residues suggests a possible role for dynamics in receptor binding and
activation. In contrast to eotaxin, eotaxin-3 exhibits no substantial mobility
on the microsecond to millisecond time scale.
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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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I.Díaz-Moreno,
D.Hollingworth,
G.Kelly,
S.Martin,
M.García-Mayoral,
P.Briata,
R.Gherzi,
and
A.Ramos
(2010).
Orientation of the central domains of KSRP and its implications for the interaction with the RNA targets.
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Nucleic Acids Res,
38,
5193-5205.
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I.Díaz-Moreno,
D.Hollingworth,
T.A.Frenkiel,
G.Kelly,
S.Martin,
S.Howell,
M.García-Mayoral,
R.Gherzi,
P.Briata,
and
A.Ramos
(2009).
Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding.
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Nat Struct Mol Biol,
16,
238-246.
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PDB code:
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J.Hol,
A.M.Küchler,
F.E.Johansen,
B.Dalhus,
G.Haraldsen,
and
I.Oynebråten
(2009).
Molecular requirements for sorting of the chemokine interleukin-8/CXCL8 to endothelial Weibel-Palade bodies.
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J Biol Chem,
284,
23532-23539.
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I.V.Nesmelova,
Y.Sham,
J.Gao,
and
K.H.Mayo
(2008).
CXC and CC Chemokines Form Mixed Heterodimers: ASSOCIATION FREE ENERGIES FROM MOLECULAR DYNAMICS SIMULATIONS AND EXPERIMENTAL CORRELATIONS.
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J Biol Chem,
283,
24155-24166.
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E.L.Wise,
C.Duchesnes,
P.C.da Fonseca,
R.A.Allen,
T.J.Williams,
and
J.E.Pease
(2007).
Small molecule receptor agonists and antagonists of CCR3 provide insight into mechanisms of chemokine receptor activation.
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J Biol Chem,
282,
27935-27943.
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M.F.García-Mayoral,
D.Hollingworth,
L.Masino,
I.Díaz-Moreno,
G.Kelly,
R.Gherzi,
C.F.Chou,
C.Y.Chen,
and
A.Ramos
(2007).
The structure of the C-terminal KH domains of KSRP reveals a noncanonical motif important for mRNA degradation.
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Structure,
15,
485-498.
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PDB codes:
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O.K.Baryshnikova,
and
B.D.Sykes
(2006).
Backbone dynamics of SDF-1alpha determined by NMR: interpretation in the presence of monomer-dimer equilibrium.
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Protein Sci,
15,
2568-2578.
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V.Petkovic,
C.Moghini,
S.Paoletti,
M.Uguccioni,
and
B.Gerber
(2004).
Eotaxin-3/CCL26 is a natural antagonist for CC chemokine receptors 1 and 5. A human chemokine with a regulatory role.
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J Biol Chem,
279,
23357-23363.
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K.L.Mayer,
and
M.J.Stone
(2003).
Backbone dynamics of the CC-chemokine eotaxin-2 and comparison among the eotaxin group chemokines.
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Proteins,
50,
184-191.
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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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