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1eih
From Proteopedia
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[[Image:1eih.jpg|left|200px]] | [[Image:1eih.jpg|left|200px]] | ||
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'''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE EOTAXIN-2''' | '''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE EOTAXIN-2''' | ||
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[[Category: Mayer, K L.]] | [[Category: Mayer, K L.]] | ||
[[Category: Stone, M J.]] | [[Category: Stone, M J.]] | ||
| - | [[Category: | + | [[Category: Chemokine]] |
| - | [[Category: | + | [[Category: Chemotactic cytokine]] |
| - | [[Category: | + | [[Category: Eosinophil chemoattractant]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:08:33 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:08, 2 May 2008
SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE EOTAXIN-2
Overview
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.
About this Structure
1EIH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2., Mayer KL, Stone MJ, Biochemistry. 2000 Jul 25;39(29):8382-95. PMID:10913244 Page seeded by OCA on Fri May 2 15:08:33 2008
