View source for 2rng


==Solution structure of big defensin==
<StructureSection load='2rng' size='340' side='right'caption='[[2rng]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rng]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2RNG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 25 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=2rng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rng OCA], [https://pdbe.org/2rng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rng RCSB], [https://www.ebi.ac.uk/pdbsum/2rng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rng ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BDEF_TACTR BDEF_TACTR] Significantly inhibits the growth of Gram-negative and Gram-positive bacteria and fungi in vitro.<ref>PMID:8586631</ref> 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2rng" style="background-color:#fffaf0;"></div>

==See Also==
*[[Defensin 3D structures|Defensin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tachypleus tridentatus]]
[[Category: Aizawa T]]
[[Category: Demura M]]
[[Category: Fujitani N]]
[[Category: Kawabata S]]
[[Category: Kawano K]]
[[Category: Kouno T]]
[[Category: Mizuguchi M]]
[[Category: Nishimura S]]
[[Category: Nitta K]]
[[Category: Osaki T]]