3n52: Difference between revisions
New page: '''Unreleased structure''' The entry 3n52 is ON HOLD Authors: Rajasekaran, Deepa Description: crystal Structure analysis of MIP2 ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] ... |
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The | ==crystal Structure analysis of MIP2== | ||
<StructureSection load='3n52' size='340' side='right'caption='[[3n52]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3n52]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3N52 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=3n52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n52 OCA], [https://pdbe.org/3n52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n52 RCSB], [https://www.ebi.ac.uk/pdbsum/3n52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n52 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CXCL2_MOUSE CXCL2_MOUSE] Chemotactic for human polymorphonuclear leukocytes but does not induce chemokinesis or an oxidative burst. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3n52" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[C-X-C motif chemokine 3D structures|C-X-C motif chemokine 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Rajasekaran D]] | |||
Latest revision as of 09:31, 27 November 2024
crystal Structure analysis of MIP2crystal Structure analysis of MIP2
Structural highlights
FunctionCXCL2_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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