1g2s
From Proteopedia
(New page: 200px<br /> <applet load="1g2s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g2s" /> '''SOLUTION STRUCTURE OF EOTAXIN-3'''<br /> =...) |
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'''SOLUTION STRUCTURE OF EOTAXIN-3'''<br /> | '''SOLUTION STRUCTURE OF EOTAXIN-3'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G2S 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:// | + | 1G2S 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=1G2S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: beta-beta-beta-alpha helix]] | [[Category: beta-beta-beta-alpha helix]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:50:32 2008'' |
Revision as of 13:50, 15 February 2008
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SOLUTION STRUCTURE OF EOTAXIN-3
Overview
Eotaxin-3 is one of three related chemokines that specifically activate, chemokine receptor CCR3. We report the 3D structure and backbone dynamics, of eotaxin-3 determined by NMR spectroscopy. Eotaxin-3 is monomeric under, the conditions in this study and consists of an unstructured N-terminus, before the first two conserved cysteine residues, an irregularly, structured N-loop following the second conserved cysteine, a single turn, of 3(10)-helix, a three-stranded antiparallel beta-sheet, an alpha-helix, and an unstructured C-terminal tail. As in other chemokines, the, alpha-helix packs against one face of the beta-sheet. The average backbone, and heavy atom rmsd values of the 20 structures (residues 9-65) are 0.44, and 1.01 A, respectively. A comparison between the structures of eotaxin-3, and related chemokines suggests that the electrostatic potential in the, vicinity of a surface groove and the structure of the beta2-beta3 turn may, be important for maintaining receptor specificity. The backbone dynamics, of eotaxin-3 were determined from 15N NMR relaxation data using the, extended model free dynamics formalism. Large amplitude motions on the, picosecond to nanosecond time scale were observed in both termini and in, some residues in the N-loop, the beta1-beta2 turn, and the beta3 strand;, the location of these residues suggests a possible role for dynamics in, receptor binding and activation. In contrast to eotaxin, eotaxin-3, exhibits no substantial mobility on the microsecond to millisecond time, scale.
About this Structure
1G2S is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
NMR solution structure and backbone dynamics of the CC chemokine eotaxin-3., Ye J, Mayer KL, Mayer MR, Stone MJ, Biochemistry. 2001 Jul 3;40(26):7820-31. PMID:11425309
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