Solution Structure of Eotaxin: A Chemokine that Selectively
Recruits Eosinophils in Allergic Inflammation

Chemoattractant Cytokine (Chemokine)Specific chemoattractant for Eosinophils, Selectively binds CCR3

Solution Nmr Structure Of Eotaxin, Minimized Average Structure

Solution Structure Of Eotaxin, An Ensemble Of 32 Nmr Solution Structures

Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Wed Jul 13 15:19:33 2011

Crump, M. P., Rajarathnam, K., Kim, K.-S., and Sykes, B. D.,
"Solution Structure of Eotaxin: a Chemokine That Selectively
Recruits Eosinophils in Allergic Inflammation," J. Biol. Chem.
273, 22471-22479 (1998).

Solution structure of eotaxin, a chemokine that selectively recruits eosinophils in allergic inflammation.

A considerable degree of variability exists in the way that 1H, 13C and 15N
chemical shifts are reported and referenced for biomolecules. In this article
we explore some of the reasons for this situation and propose guidelines for
future chemical shift referencing and for conversion from many common 1H, 13C
and 15N chemical shift standards, now used in biomolecular NMR, to those
proposed here.

Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J.,
Oldfield, E., Markley, J. L., and Sykes, B. D.
J. Biomol. NMR 6, 135-140 (1995).

1H, 13C and 15N chemical shift referencing in biomolecular NMR.

Coupling Constants were calculated from an HNHA experiment.
Residues not reported were either not observed or overlapped.

Structural Basis Of Receptor Sulfotyrosine Recognition By A Cc Chemokine: The N-terminal Region Of Ccr3 Bound To Ccl11/eotaxin-

chemokine (C-C motif) ligand 11 [synthetic construct]

Chemokine (C-C motif) ligand 11 [Homo sapiens]

PREDICTED: eotaxin-like [Gorilla gorilla gorilla]

RecName: Full=Eotaxin; AltName: Full=C-C motif chemokine 11; AltName: Full=Eosinophil chemotactic protein; AltName: Full=Small-

Eotaxin was synthesised by step-wise solid phase methods using
tBoc protection chemistry. After hydrogen fluoride deprotection,
the polypeptide was folded and purified by reverse phase HPLC as
described by Clark-Lewis et al. (Clark-Lewis, I., Vo, L., Owen, P.,
and Anderson, J. (1997) Methods Enzymol. 287, 233-250. HPLC of the
resulting product revealed a major peak and a significant minor peak
which could not be resolved by re-chromatography. The major peak was
resolved by ion-exchange chromatography on a sulfonic acid silica column.

The 13C HSQC was collected to check methyl proton

13C/1H shifts. The 13C eotaxin shifts are not reported

The pH and temperature conditions were optimised in a series
of 1D experiments with unlabelled protein to give predominantly a
monomeric species. The same conditions were therefore chosen for use
with the recombinant 15N labelled sample.