View source for 2gw9


==High-resolution solution structure of the mouse defensin Cryptdin4==
<StructureSection load='2gw9' size='340' side='right'caption='[[2gw9]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2gw9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GW9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 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=2gw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gw9 OCA], [https://pdbe.org/2gw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gw9 RCSB], [https://www.ebi.ac.uk/pdbsum/2gw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gw9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DEFA4_MOUSE DEFA4_MOUSE] Probably contributes to the antimicrobial barrier function of the small bowel mucosa.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
alpha-Defensins are mediators of mammalian innate immunity, and knowledge of their structure-function relationships is essential for understanding their mechanisms of action. We report here the NMR solution structures of the mouse Paneth cell alpha-defensin cryptdin-4 (Crp4) and a mutant (E15D)-Crp4 peptide, in which a conserved Glu(15) residue was replaced by Asp. Structural analysis of the two peptides confirms the involvement of this Glu in a conserved salt bridge that is removed in the mutant because of the shortened side chain. Despite disruption of this structural feature, the peptide variant retains a well defined native fold because of a rearrangement of side chains, which result in compensating favorable interactions. Furthermore, salt bridge-deficient Crp4 mutants were tested for bactericidal effects and resistance to proteolytic degradation, and all of the variants had similar bactericidal activities and stability to proteolysis. These findings support the conclusion that the function of the conserved salt bridge in Crp4 is not linked to bactericidal activity or proteolytic stability of the mature peptide.

Structural and functional characterization of the conserved salt bridge in mammalian paneth cell alpha-defensins: solution structures of mouse CRYPTDIN-4 and (E15D)-CRYPTDIN-4.,Rosengren KJ, Daly NL, Fornander LM, Jonsson LM, Shirafuji Y, Qu X, Vogel HJ, Ouellette AJ, Craik DJ J Biol Chem. 2006 Sep 22;281(38):28068-78. Epub 2006 Jul 20. PMID:16857681<ref>PMID:16857681</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2gw9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Craik DJ]]
[[Category: Daly NL]]
[[Category: Ouellette AJ]]
[[Category: Rosengren KJ]]
[[Category: Vogel HJ]]