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PDBsum entry 1g2s
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Nmr solution structure and backbone dynamics of the cc chemokine eotaxin-3.
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Authors
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J.Ye,
K.L.Mayer,
M.R.Mayer,
M.J.Stone.
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Ref.
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Biochemistry, 2001,
40,
7820-7831.
[DOI no: ]
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PubMed id
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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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