2mlt: Difference between revisions
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<StructureSection load='2mlt' size='340' side='right'caption='[[2mlt]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2mlt' size='340' side='right'caption='[[2mlt]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mlt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2mlt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mlt 1mlt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MLT FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2mlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlt OCA], [https://pdbe.org/2mlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mlt RCSB], [https://www.ebi.ac.uk/pdbsum/2mlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlt ProSAT]</span></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=2mlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mlt OCA], [https://pdbe.org/2mlt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mlt RCSB], [https://www.ebi.ac.uk/pdbsum/2mlt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mlt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://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> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Apis mellifera]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Eisenberg | [[Category: Eisenberg D]] | ||
[[Category: Gribskov | [[Category: Gribskov M]] | ||
[[Category: Terwilliger | [[Category: Terwilliger TC]] | ||
Latest revision as of 14:57, 22 November 2023
MELITTINMELITTIN
Structural highlights
FunctionMEL_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
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