4mgp: Difference between revisions
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== | ==Structure of racemic Ala-(8,13,18) Magainin 2== | ||
[[http://www.uniprot.org/uniprot/MAGA_XENLA MAGA_XENLA | <StructureSection load='4mgp' size='340' side='right'caption='[[4mgp]], [[Resolution|resolution]] 1.75Å' 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]] 1.75Å</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. | |||
<div style="background-color:#fffaf0;"> | |||
== 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> | |||
[[Category: | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4mgp" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Magainin 2|Magainin 2]] | ||
[[Category: | == References == | ||
[[Category: | <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]] | |||
Latest revision as of 16:37, 20 September 2023
Structure of racemic Ala-(8,13,18) Magainin 2
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