2rq2: Difference between revisions
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New page: '''Unreleased structure''' The entry 2rq2 is ON HOLD Authors: Kouno, T., Mizuguchi, M., Aizawa, T., Shinoda, H., Demura, M., Kawabata, S., Kawano, K. Description: The solution structur... |
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The | ==The solution structure of the N-terminal fragment of big defensin== | ||
<StructureSection load='2rq2' size='340' side='right'caption='[[2rq2]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2rq2]] 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=2RQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=2rq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rq2 OCA], [https://pdbe.org/2rq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rq2 RCSB], [https://www.ebi.ac.uk/pdbsum/2rq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rq2 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. 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2rq2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Tachypleus tridentatus]] | |||
[[Category: Aizawa T]] | |||
[[Category: Demura M]] | |||
[[Category: Kawabata S]] | |||
[[Category: Kawano K]] | |||
[[Category: Kouno T]] | |||
[[Category: Mizuguchi M]] | |||
[[Category: Shinoda H]] | |||
