Functional and structural studies of a Phospholipase A₂-like protein complexed to zinc ions: Insights on its myotoxicity and inhibition mechanism

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• 作者：Rafael J. Borges^a ; F&aacute ; bio F. Cardoso^a ; Carlos A.H. Fernandes^a ; Thiago R. Dreyer^a ; Delkia S. de Moraes^b ; Rafael S. Floriano^b ; L&eacute ; a Rodrigues-Simioni^b ; Marcos R.M. Fontes^a ; ^{fontes@ibb.unesp.br}
• 关键词：Phospholipase A2 ; PLA2 ; Membrane-Docking Site ; MDoS ; Membrane-Disruption Site ; MDiS ; Bothropstoxin I ; BthTX-I ; Phrenic nerve-diaphragm ; PND ; Resting potential ; RP ; Polyethylene glycol ; PEG ; PEG4000 ; PEG4k ; Protein Data Bank identification code ; PDB id ; Root-mean square deviation ; RMSD ; p-bromophenacyl bromide ; BPB
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1861
• 期：1
• 页码：3199-3209
• 全文大小：1467 K
• 卷排序：1861

文摘

Zinc ions inhibit phospholipase A2-like toxins by interaction with two different sites. Zinc ions prevent membrane disruption by the interacting with toxin C-termini. Zinc ions impair the toxin state transition leading to its inhibition. The structural transition between different toxin states was fully described. A comprehensive hypothesis for myotoxic mechanism composed by 7 steps is proposed.