3i5w: Difference between revisions
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New page: '''Unreleased structure''' The entry 3i5w is ON HOLD Authors: Pazgier, M., Lu, W. Description: Crystal structure of human alpha-defensin 5 (mutant R13H) ''Page seeded by [http://oca.w... |
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==Crystal structure of human alpha-defensin 5 (mutant R13H)== | |||
<StructureSection load='3i5w' size='340' side='right'caption='[[3i5w]], [[Resolution|resolution]] 1.63Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3i5w]] is a 2 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=3I5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I5W 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]] 1.63Å</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=FLC:CITRATE+ANION'>FLC</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=3i5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i5w OCA], [https://pdbe.org/3i5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i5w RCSB], [https://www.ebi.ac.uk/pdbsum/3i5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i5w ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DEF5_HUMAN DEF5_HUMAN] Has antimicrobial activity against Gram-negative and Gram-positive bacteria. Defensins are thought to kill microbes by permeabilizing their plasma membrane. All DEFA5 peptides exert antimicrobial activities, but their potency is affected by peptide processing.<ref>PMID:12021776</ref> <ref>PMID:15616305</ref> <ref>PMID:17088326</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Defensins constitute a major family of natural antimicrobial peptides that protect the host against microbial invasion. Here, we report on the antibacterial properties and cellular interaction of Human Defensin 5 as a function of its positive charge and hydrophobicity. We find that selective replacement of arginine residues in HD-5 by alanine or charge-neutral lysine residues reduces antibacterial killing as well as host cell interaction. We identify arginines at positions 9 and 28 in the HD-5 sequence as particularly important for its function. Replacement of arginine at position 13 to Histidine, as observed in a Crohn's disease patient, reduced bacterial killing strain-selectively. Finally, we find that HD-5 interacts with host cells via receptor-mediated mechanisms. | |||
Selective arginines are important for the antibacterial activity and host cell interaction of human alpha-defensin 5.,de Leeuw E, Rajabi M, Zou G, Pazgier M, Lu W FEBS Lett. 2009 Aug 6;583(15):2507-12. Epub 2009 Jul 7. PMID:19589339<ref>PMID:19589339</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3i5w" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Defensin 3D structures|Defensin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Lu W]] | |||
[[Category: Pazgier M]] | |||
Latest revision as of 11:27, 2 August 2023
Crystal structure of human alpha-defensin 5 (mutant R13H)
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