2ks4
NMR structure of the sea anemone actinoporin SticholysinNMR structure of the sea anemone actinoporin Sticholysin
Structural highlights
Function[ACTP1_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 (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSticholysin I is an actinoporin, a pore forming toxin, of 176 aminoacids produced by the sea anemone Stichodactyla heliantus. Isotopically labelled (13)C/(15)N recombinant protein was produced in E. coli. Here we report the complete NMR (15)N, (13)C and (1)H chemical shifts assignments of Stn I at pH 4.0 and 25 degrees C (BMRB No. 15927). 1H, 13C, and 15N NMR assignments of the actinoporin Sticholysin I.,Castrillo I, Alegre-Cebollada J, del Pozo AM, Gavilanes JG, Santoro J, Bruix M Biomol NMR Assign. 2009 Jun;3(1):5-7. Epub 2008 Nov 6. PMID:19636934[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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