2l38

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Current revision (06:52, 1 May 2024) (edit) (undo)
 
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==R29Q Sticholysin II mutant==
==R29Q Sticholysin II mutant==
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<StructureSection load='2l38' size='340' side='right'caption='[[2l38]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2l38' size='340' side='right'caption='[[2l38]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2l38]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Stihl Stihl]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ks3 2ks3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L38 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2l38]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Stichodactyla_helianthus Stichodactyla helianthus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2ks3 2ks3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L38 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gwy|1gwy]], [[1iaz|1iaz]], [[1kd6|1kd6]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2l38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l38 OCA], [https://pdbe.org/2l38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l38 RCSB], [https://www.ebi.ac.uk/pdbsum/2l38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l38 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=2l38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l38 OCA], [https://pdbe.org/2l38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l38 RCSB], [https://www.ebi.ac.uk/pdbsum/2l38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l38 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ACTP2_STOHE ACTP2_STOHE]] Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of several monomers. Cytolytic effects include red blood cells hemolysis, platelet aggregation and lysis, cytotoxic and cytostatic effects on fibroblasts. Lethality in mammals has been ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia, and inotropic effects.<ref>PMID:10978735</ref> <ref>PMID:11478962</ref>
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[https://www.uniprot.org/uniprot/ACTP2_STIHL ACTP2_STIHL] Pore-forming protein that forms cations-selective hydrophilic pores of around 1 nm and causes cardiac stimulation and hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of several monomers. Cytolytic effects include red blood cells hemolysis, platelet aggregation and lysis, cytotoxic and cytostatic effects on fibroblasts. Lethality in mammals has been ascribed to severe vasospasm of coronary vessels, cardiac arrhythmia, and inotropic effects.<ref>PMID:10978735</ref> <ref>PMID:11478962</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Stihl]]
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[[Category: Stichodactyla helianthus]]
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[[Category: Alegre-Cebollada, J]]
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[[Category: Alegre-Cebollada J]]
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[[Category: Bruix, M]]
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[[Category: Bruix M]]
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[[Category: Castrillo, I]]
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[[Category: Castrillo I]]
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[[Category: Gavilanes, J]]
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[[Category: Gavilanes J]]
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[[Category: Martinez-del-Pozo, A]]
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[[Category: Martinez-del-Pozo A]]
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[[Category: Actinoporin]]
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[[Category: Pore forming toxin]]
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[[Category: Sticholysin]]
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[[Category: Toxin]]
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Current revision

R29Q Sticholysin II mutant

PDB ID 2l38

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