4MGP
Structure of racemic Ala-(8,13,18) Magainin 2
Summary for 4MGP
| Entry DOI | 10.2210/pdb4mgp/pdb |
| Related | 1DUM 2MAG |
| Descriptor | Magainin 2 Derivative (2 entities in total) |
| Functional Keywords | phenylalanine zipper, antimicrobial protein |
| Biological source | Xenopus laevis (clawed frog,common platanna,platanna) |
| Cellular location | Secreted: P11006 |
| Total number of polymer chains | 1 |
| Total formula weight | 2483.99 |
| Authors | Hayouka, Z.,Mortenson, D.E.,Kreitler, D.F.,Weisblum, B.,Gellman, S.H.,Forest, K.T. (deposition date: 2013-08-28, release date: 2013-10-16, Last modification date: 2023-09-20) |
| Primary citation | Hayouka, Z.,Mortenson, D.E.,Kreitler, D.F.,Weisblum, B.,Forest, K.T.,Gellman, S.H. Evidence for Phenylalanine Zipper-Mediated Dimerization in the X-ray Crystal Structure of a Magainin 2 Analogue. J.Am.Chem.Soc., 135:15738-15741, 2013 Cited by PubMed Abstract: 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. PubMed: 24102563DOI: 10.1021/ja409082w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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