3n52: Difference between revisions
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==crystal Structure analysis of MIP2== | ==crystal Structure analysis of MIP2== | ||
<StructureSection load='3n52' size='340' side='right' caption='[[3n52]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3n52' size='340' side='right' caption='[[3n52]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3n52]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3n52]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N52 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cxcl2, Mip-2, Mip2, Scyb2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cxcl2, Mip-2, Mip2, Scyb2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3n52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n52 RCSB], [http://www.ebi.ac.uk/pdbsum/3n52 PDBsum]</span></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=3n52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n52 OCA], [http://pdbe.org/3n52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n52 RCSB], [http://www.ebi.ac.uk/pdbsum/3n52 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n52 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3n52" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Lk3 transgenic mice]] | ||
[[Category: Rajasekaran, D]] | [[Category: Rajasekaran, D]] | ||
[[Category: Cxcl2]] | [[Category: Cxcl2]] | ||
Revision as of 12:23, 4 August 2016
crystal Structure analysis of MIP2crystal Structure analysis of MIP2
Structural highlights
Function[CXCL2_MOUSE] Chemotactic for human polymorphonuclear leukocytes but does not induce chemokinesis or an oxidative burst. Publication Abstract from PubMedMIP-2/CXCL2 is a murine chemokine related to human chemokines that possesses the Glu-Leu-Arg (ELR) activation motif and activates CXCR2 for neutrophil chemotaxis. We determined the structure of MIP-2 to 1.9 A resolution and created a model with its murine receptor CXCR2 based on the coordinates of human CXCR4. Chemokine-induced migration of cells through specific G-protein coupled receptors is regulated by glycosaminoglycans (GAGs) that oligomerize chemokines. MIP-2 GAG-binding residues were identified that interact with heparin disaccharide I-S by NMR spectroscopy. A model GAG/MIP-2/CXCR2 complex that supports a 2:2 complex between chemokine and receptor was created. Mutants of these disaccharide-binding residues were made and tested for heparin binding, in vitro neutrophil chemotaxis, and in vivo neutrophil recruitment to the mouse peritoneum and lung. The mutants have a 10-fold decrease in neutrophil chemotaxis in vitro. There is no difference in neutrophil recruitment between wild-type MIP-2 and mutants in the peritoneum, but all activity of the mutants is lost in the lung, supporting the concept that GAG regulation of chemokines is tissue-dependent. A Model of GAG/MIP-2/CXCR2 Interfaces and Its Functional Effects.,Rajasekaran D, Keeler C, Syed MA, Jones MC, Harrison JK, Wu D, Bhandari V, Hodsdon ME, Lolis EJ Biochemistry. 2012 Jul 2. PMID:22686371[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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