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3i5w
From Proteopedia
(Difference between revisions)
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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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3I5W FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zmp|1zmp]], [[3gny|3gny]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3i5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i5w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3i5w RCSB], [http://www.ebi.ac.uk/pdbsum/3i5w PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | ||
==See Also== | ==See Also== | ||
*[[Defensin|Defensin]] | *[[Defensin|Defensin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: Lu, W | + | </StructureSection> |
| - | [[Category: Pazgier, M | + | [[Category: Lu, W]] |
| + | [[Category: Pazgier, M]] | ||
[[Category: Antibiotic]] | [[Category: Antibiotic]] | ||
[[Category: Antimicrobial]] | [[Category: Antimicrobial]] | ||
Revision as of 06:33, 18 December 2014
Crystal structure of human alpha-defensin 5 (mutant R13H)
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