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4k09
From Proteopedia
(Difference between revisions)
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<StructureSection load='4k09' size='340' side='right'caption='[[4k09]], [[Resolution|resolution]] 2.11Å' scene=''> | <StructureSection load='4k09' size='340' side='right'caption='[[4k09]], [[Resolution|resolution]] 2.11Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4k09]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4k09]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bothrops_brazili Bothrops brazili]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K09 FirstGlance]. <br> |
| - | </td></tr> | + | </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=4k09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k09 OCA], [https://pdbe.org/4k09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k09 RCSB], [https://www.ebi.ac.uk/pdbsum/4k09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k09 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PA2H1_BOTBZ PA2H1_BOTBZ] Snake venom phospholipase A2 homolog that lacks enzymatic activity. Is myotoxic and displays edema-inducing activities in mouse paw (PubMed:18602430). Also displays cytotoxic activity against some cell lines, and antimicrobial activities against E.coli, C.albicans and Leishmania (PubMed:18602430). A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g. fatty acid) at the hydrophobic channel of the protein leading to a reorientation of a monomer (PubMed:24145104). This reorientation causes a transition between 'inactive' to 'active' states, causing alignment of C-terminal and membrane-docking sites (MDoS) side-by-side and putting the membrane-disruption sites (MDiS) in the same plane, exposed to solvent and in a symmetric position for both monomers (PubMed:24145104). The MDoS region stabilizes the toxin on membrane by the interaction of charged residues with phospholipid head groups (PubMed:24145104). Subsequently, the MDiS region destabilizes the membrane with penetration of hydrophobic residues (PubMed:24145104). This insertion causes a disorganization of the membrane, allowing an uncontrolled influx of ions (i.e. calcium and sodium), and eventually triggering irreversible intracellular alterations and cell death (PubMed:24145104).<ref>PMID:18602430</ref> <ref>PMID:24145104</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Bothrops brazili]] | [[Category: Bothrops brazili]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Borges | + | [[Category: Borges RJ]] |
| - | [[Category: Comparetti | + | [[Category: Comparetti EJ]] |
| - | [[Category: Fernandes | + | [[Category: Fernandes CAH]] |
| - | [[Category: Fontes | + | [[Category: Fontes MRM]] |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of BbTX-II from Bothrops brazili venom
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