2mlt

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MELITTINMELITTIN

Structural highlights

2mlt is a 2 chain structure with sequence from Apis mellifera. This structure supersedes the now removed PDB entry 1mlt. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MEL_APIME Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.[1] Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.[2]

References

  1. Sciani JM, Marques-Porto R, Lourenco Junior A, Orsi Rde O, Ferreira Junior RS, Barraviera B, Pimenta DC. Identification of a novel melittin isoform from Africanized Apis mellifera venom. Peptides. 2010 Aug;31(8):1473-9. doi: 10.1016/j.peptides.2010.05.001. Epub 2010, May 21. PMID:20472009 doi:http://dx.doi.org/10.1016/j.peptides.2010.05.001
  2. Sciani JM, Marques-Porto R, Lourenco Junior A, Orsi Rde O, Ferreira Junior RS, Barraviera B, Pimenta DC. Identification of a novel melittin isoform from Africanized Apis mellifera venom. Peptides. 2010 Aug;31(8):1473-9. doi: 10.1016/j.peptides.2010.05.001. Epub 2010, May 21. PMID:20472009 doi:http://dx.doi.org/10.1016/j.peptides.2010.05.001

2mlt, resolution 2.00Å

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