1f2l

From Proteopedia

(Difference between revisions)

Revision as of 09:22, 27 December 2017

CRYSTAL STRUCTURE OF CHEMOKINE DOMAIN OF FRACTALKINE

Structural highlights

1f2l is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f2l"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF CHEMOKINE DOMAIN OF FRACTALKINE==
 <StructureSection load='1f2l' size='340' side='right' caption='[[1f2l]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == 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>
-</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]</span></td></tr>
+</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>
 </table>
 == Function ==
@@ Line 11: / Line 12: @@
 Check<jmol>
   <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>
     <text>to colour the structure by Evolutionary Conservation</text>

1f2l

From Proteopedia

Revision as of 09:22, 27 December 2017

CRYSTAL STRUCTURE OF CHEMOKINE DOMAIN OF FRACTALKINE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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