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==Solution structure of big defensin== | |||
=== | <StructureSection load='2rng' size='340' side='right' caption='[[2rng]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2rng]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RNG FirstGlance]. <br> | |||
</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=2rng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rng OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rng RCSB], [http://www.ebi.ac.uk/pdbsum/2rng PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Big defensin is a 79-residue peptide derived from hemocytes of the Japanese horseshoe crab. It has antimicrobial activities against Gram-positive and -negative bacteria. The amino acid sequence of big defensin can be divided into an N-terminal hydrophobic half and a C-terminal cationic half. Interestingly, the trypsin cleaves big defensin into two fragments, the N-terminal and C-terminal fragments, which are responsible for antimicrobial activity against Gram-positive and -negative bacteria, respectively. To explore the antimicrobial mechanism of big defensin, we determined the solution structure of mature big defensin and performed a titration experiment with DPC micelles. Big defensin has a novel defensin structure; the C-terminal domain adopts a beta-defensin structure, and the N-terminal domain forms a unique globular conformation. It is noteworthy that the hydrophobic N-terminal domain undergoes a conformational change in micelle solution, while the C-terminal domain remains unchanged. Here, we propose that the N-terminal domain achieves its antimicrobial activity in a novel fashion and explain that big defensin has developed a strategy different from those of other beta-defensins to suppress the growth of Gram-positive bacteria. | |||
A novel beta-defensin structure: a potential strategy of big defensin for overcoming resistance by Gram-positive bacteria.,Kouno T, Fujitani N, Mizuguchi M, Osaki T, Nishimura S, Kawabata S, Aizawa T, Demura M, Nitta K, Kawano K Biochemistry. 2008 Oct 7;47(40):10611-9. Epub 2008 Sep 12. PMID:18785751<ref>PMID:18785751</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__ | |||
</StructureSection> | |||
[[Category: Tachypleus tridentatus]] | [[Category: Tachypleus tridentatus]] | ||
[[Category: Aizawa, T | [[Category: Aizawa, T]] | ||
[[Category: Demura, M | [[Category: Demura, M]] | ||
[[Category: Fujitani, N | [[Category: Fujitani, N]] | ||
[[Category: Kawabata, S | [[Category: Kawabata, S]] | ||
[[Category: Kawano, K | [[Category: Kawano, K]] | ||
[[Category: Kouno, T | [[Category: Kouno, T]] | ||
[[Category: Mizuguchi, M | [[Category: Mizuguchi, M]] | ||
[[Category: Nishimura, S | [[Category: Nishimura, S]] | ||
[[Category: Nitta, K | [[Category: Nitta, K]] | ||
[[Category: Osaki, T | [[Category: Osaki, T]] | ||
[[Category: Alpha-helices & beta-sheet]] | [[Category: Alpha-helices & beta-sheet]] | ||
[[Category: Antibiotic]] | [[Category: Antibiotic]] | ||
Revision as of 17:07, 17 December 2014
Solution structure of big defensinSolution structure of big defensin
Structural highlights
Publication Abstract from PubMedBig defensin is a 79-residue peptide derived from hemocytes of the Japanese horseshoe crab. It has antimicrobial activities against Gram-positive and -negative bacteria. The amino acid sequence of big defensin can be divided into an N-terminal hydrophobic half and a C-terminal cationic half. Interestingly, the trypsin cleaves big defensin into two fragments, the N-terminal and C-terminal fragments, which are responsible for antimicrobial activity against Gram-positive and -negative bacteria, respectively. To explore the antimicrobial mechanism of big defensin, we determined the solution structure of mature big defensin and performed a titration experiment with DPC micelles. Big defensin has a novel defensin structure; the C-terminal domain adopts a beta-defensin structure, and the N-terminal domain forms a unique globular conformation. It is noteworthy that the hydrophobic N-terminal domain undergoes a conformational change in micelle solution, while the C-terminal domain remains unchanged. Here, we propose that the N-terminal domain achieves its antimicrobial activity in a novel fashion and explain that big defensin has developed a strategy different from those of other beta-defensins to suppress the growth of Gram-positive bacteria. A novel beta-defensin structure: a potential strategy of big defensin for overcoming resistance by Gram-positive bacteria.,Kouno T, Fujitani N, Mizuguchi M, Osaki T, Nishimura S, Kawabata S, Aizawa T, Demura M, Nitta K, Kawano K Biochemistry. 2008 Oct 7;47(40):10611-9. Epub 2008 Sep 12. PMID:18785751[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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