2l38 | pdb_00002l38

R29Q Sticholysin II mutant

spinqualitylabelsall models 2l38, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2l38 is a 1 chain structure with sequence from Stihl. This structure supersedes the now removed PDB entry 2ks3. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1gwy, 1iaz, 1kd6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also Cytolysin

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