3qte

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<StructureSection load='3qte' size='340' side='right'caption='[[3qte]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3qte' size='340' side='right'caption='[[3qte]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qte]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QTE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qte]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QTE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.949&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zmq|1zmq]], [[1zmp|1zmp]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3qte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qte OCA], [https://pdbe.org/3qte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qte RCSB], [https://www.ebi.ac.uk/pdbsum/3qte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qte ProSAT]</span></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=3qte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qte OCA], [https://pdbe.org/3qte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qte RCSB], [https://www.ebi.ac.uk/pdbsum/3qte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qte ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DEF6_HUMAN DEF6_HUMAN]] Has very low antimicrobial activity against Gram-negative and Gram-positive bacteria. May protect cells against infection with HIV-1.<ref>PMID:15616305</ref> <ref>PMID:17088326</ref>
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[https://www.uniprot.org/uniprot/DEF6_HUMAN DEF6_HUMAN] Has very low antimicrobial activity against Gram-negative and Gram-positive bacteria. May protect cells against infection with HIV-1.<ref>PMID:15616305</ref> <ref>PMID:17088326</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Defensins are antimicrobial peptides that contribute broadly to innate immunity, including protection of mucosal tissues. Human alpha-defensin (HD) 6 is highly expressed by secretory Paneth cells of the small intestine. However, in contrast to the other defensins, it lacks appreciable bactericidal activity. Nevertheless, we report here that HD6 affords protection against invasion by enteric bacterial pathogens in vitro and in vivo. After stochastic binding to bacterial surface proteins, HD6 undergoes ordered self-assembly to form fibrils and nanonets that surround and entangle bacteria. This self-assembly mechanism occurs in vivo, requires histidine-27, and is consistent with x-ray crystallography data. These findings support a key role for HD6 in protecting the small intestine against invasion by diverse enteric pathogens and may explain the conservation of HD6 throughout Hominidae evolution.
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Human alpha-defensin 6 promotes mucosal innate immunity through self-assembled peptide nanonets.,Chu H, Pazgier M, Jung G, Nuccio SP, Castillo PA, de Jong MF, Winter MG, Winter SE, Wehkamp J, Shen B, Salzman NH, Underwood MA, Tsolis RM, Young GM, Lu W, Lehrer RI, Baumler AJ, Bevins CL Science. 2012 Jul 27;337(6093):477-81. Epub 2012 Jun 21. PMID:22722251<ref>PMID:22722251</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qte" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lu, W]]
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[[Category: Lu W]]
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[[Category: Pazgier, M]]
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[[Category: Pazgier M]]
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[[Category: Antimicrobial protein]]
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[[Category: Hd6]]
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[[Category: Human alpha defensin]]
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[[Category: Paneth cells defensin]]
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Revision as of 11:57, 14 March 2024

Crystal structure of human alpha-defensin 6 (H27W mutant)

PDB ID 3qte

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