View source for 2lwl


==Structural Basis for the Interaction of Human &#946;-Defensin 6 and Its Putative Chemokine Receptor CCR2 and Breast Cancer Microvesicles==
<StructureSection load='2lwl' size='340' side='right'caption='[[2lwl]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lwl]] is a 1 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=2LWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LWL 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lwl OCA], [https://pdbe.org/2lwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lwl RCSB], [https://www.ebi.ac.uk/pdbsum/2lwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lwl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D106A_HUMAN D106A_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human beta-defensins (hBDs) are believed to function as alarm molecules that stimulate the adaptive immune system when a threat is present. In addition to its antimicrobial activity, defensins present other activities such as chemoattraction of a range of different cell types to the sites of inflammation. We have solved the structure of the hBD6 by NMR spectroscopy that contains a conserved beta-defensin domain followed by an extended C-terminus. We use NMR to monitor the interaction of hBD6 with microvesicles shed by breast cancer cell lines and with peptides derived from the extracellular domain of CC chemokine receptor 2 (Nt-CCR2) possessing or not possessing sulfation on Tyr26 and Tyr28. The NMR-derived model of the hBD6/CCR2 complex reveals a contiguous binding surface on hBD6, which comprises amino acid residues of the alpha-helix and beta2-beta3 loop. The microvesicle binding surface partially overlaps with the chemokine receptor interface. NMR spin relaxation suggests that free hBD6 and the hBD6/CCR2 complex exhibit microsecond-to-millisecond conformational dynamics encompassing the CCR2 binding site, which might facilitate selection of the molecular configuration optimal for binding. These data offer new insights into the structure-function relation of the hBD6-CCR2 interaction, which is a promising target for the design of novel anticancer agents.

Structural Basis for the Interaction of Human beta-Defensin 6 and Its Putative Chemokine Receptor CCR2 and Breast Cancer Microvesicles.,De Paula VS, Gomes NS, Lima LG, Miyamoto CA, Monteiro RQ, Almeida FC, Valente AP J Mol Biol. 2013 Aug 11. pii: S0022-2836(13)00504-4. doi:, 10.1016/j.jmb.2013.08.001. PMID:23938203<ref>PMID:23938203</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lwl" style="background-color:#fffaf0;"></div>

==See Also==
*[[Defensin 3D structures|Defensin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Almeida FCL]]
[[Category: Gomes NSF]]
[[Category: Lima LG]]
[[Category: Miyamoto CA]]
[[Category: Monteiro RQ]]
[[Category: Valente A]]
[[Category: De Paula VS]]