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[[Image:2rq2.png|left|200px]]
==The solution structure of the N-terminal fragment of big defensin==
<StructureSection load='2rq2' size='340' side='right' caption='[[2rq2]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rq2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RQ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RQ2 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=2rq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rq2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rq2 RCSB], [http://www.ebi.ac.uk/pdbsum/2rq2 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. The amino acid sequence of big defensin is divided into an N-terminal hydrophobic domain and a C-terminal cationic domain, which are responsible for antimicrobial activities against Gram-positive and -negative bacteria, respectively. The N-terminal domain of big defensin forms a unique globular conformation with two alpha-helices and a parallel beta-sheet, while the C-terminal domain adopts a beta-defensin-like fold. Although our previous study implied that big defensin changes its N-terminal structure in a micellar environment, due to the poor quality of the NMR spectra it remained to be resolved whether the N-terminal domain adopts any structure in the presence of micelles. In this analysis, we successfully determined the structure of the N-terminal fragment of big defensin in a micellar solution, showing that the fragment peptide forms a single alpha-helix structure. Moreover, NMR experiments using paramagnetic probes revealed that the N-terminal domain of big defensin penetrates into the micelle with a dipping at the N-terminal edge of the alpha-helix. Here, we propose a model for how big defensin associates with the target membrane.


{{STRUCTURE_2rq2|  PDB=2rq2  |  SCENE=  }}
A novel beta-defensin structure: big defensin changes its N-terminal structure to associate with the target membrane.,Kouno T, Mizuguchi M, Aizawa T, Shinoda H, Demura M, Kawabata S, Kawano K Biochemistry. 2009 Aug 18;48(32):7629-35. PMID:19588912<ref>PMID:19588912</ref>


===The solution structure of the N-terminal fragment of big defensin===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_19588912}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2rq2]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RQ2 OCA].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:019588912</ref><references group="xtra"/>
[[Category: Aizawa, T.]]
[[Category: Aizawa, T.]]
[[Category: Demura, M.]]
[[Category: Demura, M.]]
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