1bh1

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bh1 RCSB], [http://www.ebi.ac.uk/pdbsum/1bh1 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bh1 RCSB], [http://www.ebi.ac.uk/pdbsum/1bh1 PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/MEL_APIME 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.<ref>PMID:20472009</ref> Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.<ref>PMID:20472009</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 05:27, 25 December 2014

STRUCTURAL STUDIES OF D-PRO MELITTIN, NMR, 20 STRUCTURES

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