View source for 2mpm


==Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: the N-terminal Region of CCR3 Bound to CCL11/Eotaxin-1==
<StructureSection load='2mpm' size='340' side='right'caption='[[2mpm]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mpm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MPM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TYS:O-SULFO-L-TYROSINE'>TYS</scene></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=2mpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mpm OCA], [https://pdbe.org/2mpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mpm RCSB], [https://www.ebi.ac.uk/pdbsum/2mpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mpm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CCL11_HUMAN CCL11_HUMAN] In response to the presence of allergens, this protein directly promotes the accumulation of eosinophils, a prominent feature of allergic inflammatory reactions. Binds to CCR3.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Trafficking of leukocytes in immune surveillance and inflammatory responses is activated by chemokines engaging their receptors. Sulfation of tyrosine residues in peptides derived from the eosinophil chemokine receptor CCR3 dramatically enhances binding to cognate chemokines. We report the structural basis of this recognition and affinity enhancement. We describe the structure of a CC chemokine (CCL11/eotaxin-1) bound to a fragment of a chemokine receptor: residues 8-23 of CCR3, including two sulfotyrosine residues. We also show that intact CCR3 is sulfated and sulfation enhances receptor activity. The CCR3 sulfotyrosine residues form hydrophobic, salt bridge and cation-pi interactions with residues that are highly conserved in CC chemokines. However, the orientation of the chemokine relative to the receptor N terminus differs substantially from those observed for two CXC chemokines, suggesting that initial binding of the receptor sulfotyrosine residues guides subsequent steps in receptor activation, thereby influencing the receptor conformational changes and signaling.

Structural Basis of Receptor Sulfotyrosine Recognition by a CC Chemokine: The N-Terminal Region of CCR3 Bound to CCL11/Eotaxin-1.,Millard CJ, Ludeman JP, Canals M, Bridgford JL, Hinds MG, Clayton DJ, Christopoulos A, Payne RJ, Stone MJ Structure. 2014 Oct 23;22(11):1571-1581. doi: 10.1016/j.str.2014.08.023. PMID:25450766<ref>PMID:25450766</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mpm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bridgford JL]]
[[Category: Canals M]]
[[Category: Christopoulos A]]
[[Category: Clayton DJ]]
[[Category: Hinds MG]]
[[Category: Ludeman JP]]
[[Category: Millard CJ]]
[[Category: Payne RJ]]
[[Category: Stone MJ]]