1eig
From Proteopedia
(New page: 200px<br /> <applet load="1eig" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eig" /> '''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE E...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1eig. | + | [[Image:1eig.jpg|left|200px]]<br /><applet load="1eig" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1eig" size=" | + | |
caption="1eig" /> | caption="1eig" /> | ||
'''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE EOTAXIN-2'''<br /> | '''SOLUTION STRUCTURE OF THE HUMAN CHEMOKINE EOTAXIN-2'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1EIG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1EIG is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
| Line 20: | Line 19: | ||
[[Category: eosinophil chemoattractant]] | [[Category: eosinophil chemoattractant]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:43:33 2008'' |
Revision as of 13:43, 15 February 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
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 Fri Feb 15 15:43:33 2008
