1EIG

SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE EOTAXIN-2

Summary for 1EIG

• Entry DOI: 10.2210/pdb1eig/pdb
• Related: 1EIH
• NMR Information: BMRB: 4590
• Descriptor: EOTAXIN-2 (1 entity in total)
• Functional Keywords: chemokine, chemotactic cytokine, eosinophil chemoattractant, cytokine
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 8323.78

Authors

Mayer, K.L.,Stone, M.J. (deposition date: 2000-02-25, release date: 2000-12-06, Last modification date: 2024-11-20)

Primary citation

Mayer, K.L.,Stone, M.J.
NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2.
Biochemistry, 39:8382-8395, 2000

PubMed Abstract: The human CC chemokine eotaxin-2 is a specific agonist for the chemokine receptor CCR3 and may play a role in the recruitment of eosinophils in allergic diseases and parasitic infections. We report the solution structure of eotaxin-2 determined using heteronuclear and triple resonance NMR methods. A family of 20 structures was calculated by hybrid distance geometry-simulated annealing from 854 NOE distance restraints, 48 dihedral angle restraints, and 12 hydrogen bond restraints. The structure of eotaxin-2 (73 amino acid residues) consists of a helical turn (residues 17-20) followed by a 3-stranded antiparallel beta-sheet (residues 22-26, 37-41, and 44-49) and an alpha-helix (residues 54-66). The N-loop (residues 9-16) is packed against both the sheet and the helix with the two conserved disulfide bonds tethering the N-terminal/N-loop region to the beta-sheet. The average backbone and heavy atom rmsd values of the 20 structures (residues 7-66) are 0.52 and 1.13 A, respectively. A linear peptide corresponding to the N-terminal region of CCR3 binds to eotaxin-2, inducing concentration-dependent chemical shift changes or line broadening of many residues. The distribution of these residues suggests that the peptide binds into an extended groove located at the interface between the N-loop and the beta2-beta3 hairpin. The receptor peptide may also interact with the N-terminus of the chemokine and part of the alpha-helix. Comparison of the eotaxin-2 structure with those of related chemokines indicates several structural features that may contribute to receptor specificity.

PubMed: 10913244
DOI: 10.1021/bi000523j

Experimental method

SOLUTION NMR