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| | ==SOLUTION STRUCTURE OF EOTAXIN-3== | | ==SOLUTION STRUCTURE OF EOTAXIN-3== |
| - | <StructureSection load='1g2s' size='340' side='right'caption='[[1g2s]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1g2s' size='340' side='right'caption='[[1g2s]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1g2s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1G2S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1g2s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G2S FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1g2t|1g2t]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EOTAXIN-3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2s OCA], [https://pdbe.org/1g2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g2s RCSB], [https://www.ebi.ac.uk/pdbsum/1g2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g2s ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1g2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g2s OCA], [http://pdbe.org/1g2s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g2s RCSB], [http://www.ebi.ac.uk/pdbsum/1g2s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g2s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CCL26_HUMAN CCL26_HUMAN]] Chemotactic for eosinophils and basophils. Binds to CCR3. | + | [https://www.uniprot.org/uniprot/CCL26_HUMAN CCL26_HUMAN] Chemotactic for eosinophils and basophils. Binds to CCR3. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g2/1g2s_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g2/1g2s_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mayer, K L]] | + | [[Category: Mayer KL]] |
| - | [[Category: Mayer, M R]] | + | [[Category: Mayer MR]] |
| - | [[Category: Stone, M J]] | + | [[Category: Stone MJ]] |
| - | [[Category: Ye, J]] | + | [[Category: Ye J]] |
| - | [[Category: Beta-beta-beta-alpha helix]]
| + | |
| - | [[Category: Cytokine]]
| + | |
| Structural highlights
Function
CCL26_HUMAN Chemotactic for eosinophils and basophils. Binds to CCR3.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ye J, Mayer KL, Mayer MR, Stone MJ. NMR solution structure and backbone dynamics of the CC chemokine eotaxin-3. Biochemistry. 2001 Jul 3;40(26):7820-31. PMID:11425309
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