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Crystal structure of phospholipase PA2‐Vb, a protease‐activated receptor agonist from the Trimeresurus stejnegeri snake venom
Author(s) -
Zeng Fuxing,
Zhang Wenjuan,
Xue Nairui,
Teng Maikun,
Li Xu,
Shen Bing
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.10.032
Subject(s) - venom , biology , phospholipase c , receptor , snake venom , phospholipase a2 , phospholipase , agonist , protease , biochemistry , enzyme
Phospholipase A 2 (PLA 2 ) is an important component in snake venoms. Here, an acidic PLA 2 , designated PA2‐Vb was isolated from the Trimeresurus stejnegeri snake venom. PA2‐Vb acts on a protease‐activated receptor (PAR‐1) to evoke Ca 2+ release through the inositol 1,4,5‐trisphosphate receptor (IP 3 R) and induces mouse aorta contraction. PAR‐1, phospholipase C and IP 3 R inhibitors suppressed PA2‐Vb‐induced aorta contraction. The crystal structure reveals that PA2‐Vb has the typical fold of most snake venom PLA 2 . Several PEG molecules bond to a positively charged pocket. The finding offers a novel pharmacological basis of the structure for investigating the PAR‐1 receptor and suggests potential applications for PA2‐Vb in the vascular system.