View source for 4mgp


==Structure of racemic Ala-(8,13,18) Magainin 2==
<StructureSection load='4mgp' size='340' side='right'caption='[[4mgp]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4mgp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MGP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</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=4mgp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mgp OCA], [https://pdbe.org/4mgp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mgp RCSB], [https://www.ebi.ac.uk/pdbsum/4mgp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mgp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MAGA_XENLA MAGA_XENLA] Antimicrobial peptides that inhibit the growth of numerous species of bacteria and fungi and induce osmotic lysis of protozoa. Magainins are membrane lytic agents.
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== Publication Abstract from PubMed ==
High-resolution structure elucidation has been challenging for the large group of host-defense peptides that form helices on or within membranes but do not manifest a strong folding propensity in aqueous solution. Here we report the crystal structure of an analogue of the widely studied host-defense peptide magainin 2. Magainin 2 (S8A, G13A, G18A) is a designed variant that displays enhanced antibacterial activity relative to the natural peptide. The crystal structure of magainin 2 (S8A, G13A, G18A), obtained for the racemic form, features a dimerization mode that has previously been proposed to play a role in the antibacterial activity of magainin 2 and related peptides.

Evidence for Phenylalanine Zipper-Mediated Dimerization in the X-ray Crystal Structure of a Magainin 2 Analogue.,Hayouka Z, Mortenson DE, Kreitler DF, Weisblum B, Forest KT, Gellman SH J Am Chem Soc. 2013 Oct 8. PMID:24102563<ref>PMID:24102563</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4mgp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Magainin 2|Magainin 2]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Forest KT]]
[[Category: Gellman SH]]
[[Category: Hayouka Z]]
[[Category: Kreitler DF]]
[[Category: Mortenson DE]]
[[Category: Weisblum B]]