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| | <StructureSection load='1f2l' size='340' side='right'caption='[[1f2l]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1f2l' size='340' side='right'caption='[[1f2l]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1f2l]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F2L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1f2l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2L FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2l OCA], [http://pdbe.org/1f2l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f2l RCSB], [http://www.ebi.ac.uk/pdbsum/1f2l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2l ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=1f2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2l OCA], [https://pdbe.org/1f2l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2l RCSB], [https://www.ebi.ac.uk/pdbsum/1f2l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/X3CL1_HUMAN X3CL1_HUMAN]] The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Binds to CX3CR1.<ref>PMID:21829356</ref> | + | [https://www.uniprot.org/uniprot/X3CL1_HUMAN X3CL1_HUMAN] The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Binds to CX3CR1.<ref>PMID:21829356</ref> |
| | == 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/f2/1f2l_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f2/1f2l_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: Handel, T M]] | + | [[Category: Handel TM]] |
| - | [[Category: Hoover, D M]] | + | [[Category: Hoover DM]] |
| - | [[Category: Lubkowski, J]] | + | [[Category: Lubkowski J]] |
| - | [[Category: Mizoue, L S]] | + | [[Category: Mizoue LS]] |
| - | [[Category: Chemoattractant]]
| + | |
| - | [[Category: Cytokine]]
| + | |
| - | [[Category: Fractalkine]]
| + | |
| - | [[Category: Neurotactin]]
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| Structural highlights
Function
X3CL1_HUMAN The soluble form is chemotactic for T-cells and monocytes, but not for neutrophils. The membrane-bound form promotes adhesion of those leukocytes to endothelial cells. May play a role in regulating leukocyte adhesion and migration processes at the endothelium. Binds to CX3CR1.[1]
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
Fractalkine, or neurotactin, is a chemokine that is present in endothelial cells from several tissues, including brain, liver, and kidney. It is the only member of the CX(3)C class of chemokines. Fractalkine contains a chemokine domain (CDF) attached to a membrane-spanning domain via a mucin-like stalk. However, fractalkine can also be proteolytically cleaved from its membrane-spanning domain to release a freely diffusible form. Fractalkine attracts and immobilizes leukocytes by binding to its receptor, CX(3)CR1. The x-ray crystal structure of CDF has been solved and refined to 2.0 A resolution. The CDF monomers form a dimer through an intermolecular beta-sheet. This interaction is somewhat similar to that seen in other dimeric CC chemokine crystal structures. However, the displacement of the first disulfide in CDF causes the dimer to assume a more compact quaternary structure relative to CC chemokines, which is unique to CX(3)C chemokines. Although fractalkine can bind to heparin in vitro, as shown by comparison of electrostatic surface plots with other chemokines and by heparin chromatography, the role of this property in vivo is not well understood.
The crystal structure of the chemokine domain of fractalkine shows a novel quaternary arrangement.,Hoover DM, Mizoue LS, Handel TM, Lubkowski J J Biol Chem. 2000 Jul 28;275(30):23187-93. PMID:10770945[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Xue X, Lu Q, Wei H, Wang D, Chen D, He G, Huang L, Wang H, Wang X. Structural basis of chemokine sequestration by CrmD, a poxvirus-encoded tumor necrosis factor receptor. PLoS Pathog. 2011 Jul;7(7):e1002162. Epub 2011 Jul 28. PMID:21829356 doi:10.1371/journal.ppat.1002162
- ↑ Hoover DM, Mizoue LS, Handel TM, Lubkowski J. The crystal structure of the chemokine domain of fractalkine shows a novel quaternary arrangement. J Biol Chem. 2000 Jul 28;275(30):23187-93. PMID:10770945 doi:http://dx.doi.org/10.1074/jbc.M002584200
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