3n52

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[[Image:3n52.png|left|200px]]
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==crystal Structure analysis of MIP2==
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<StructureSection load='3n52' size='340' side='right' caption='[[3n52]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3n52]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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>
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</td></tr><tr><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 Mus musculus])</td></tr>
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<tr><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>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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MIP-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.
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{{STRUCTURE_3n52| PDB=3n52 | SCENE= }}
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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<ref>PMID:22686371</ref>
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===crystal Structure analysis of MIP2===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_22686371}}
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==See Also==
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*[[C-X-C motif chemokine|C-X-C motif chemokine]]
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==About this Structure==
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== References ==
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[[3n52]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N52 OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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<ref group="xtra">PMID:022686371</ref><references group="xtra"/>
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Rajasekaran, D.]]
[[Category: Rajasekaran, D.]]

Revision as of 05:28, 4 June 2014

crystal Structure analysis of MIP2

3n52, resolution 1.90Å

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