1eig
From Proteopedia
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| - | [[Image:1eig.jpg|left|200px]] | + | [[Image:1eig.jpg|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE EOTAXIN-2''' | + | {{Structure |
| + | |PDB= 1eig |SIZE=350|CAPTION= <scene name='initialview01'>1eig</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE EOTAXIN-2''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EIG is a [ | + | 1EIG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIG OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10913244 10913244] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: eosinophil chemoattractant]] | [[Category: eosinophil chemoattractant]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:56:02 2008'' |
Revision as of 08:56, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1EIG 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 Thu Mar 20 10:56:02 2008
