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Here, an acidic PLA\n                    <jats:sub>2<\/jats:sub>\n                    , designated PA2\u2010Vb was isolated from the\n                    <jats:italic>Trimeresurus stejnegeri<\/jats:italic>\n                    snake venom. PA2\u2010Vb acts on a protease\u2010activated receptor (PAR\u20101) to evoke Ca\n                    <jats:sup>2+<\/jats:sup>\n                    release through the inositol 1,4,5\u2010trisphosphate receptor (IP\n                    <jats:sub>3<\/jats:sub>\n                    R) and induces mouse aorta contraction. PAR\u20101, phospholipase C and IP\n                    <jats:sub>3<\/jats:sub>\n                    R inhibitors suppressed PA2\u2010Vb\u2010induced aorta contraction. The crystal structure reveals that PA2\u2010Vb has the typical fold of most snake venom PLA\n                    <jats:sub>2<\/jats:sub>\n                    . Several PEG molecules bond to a positively charged pocket. The finding offers a novel pharmacological basis of the structure for investigating the PAR\u20101 receptor and suggests potential applications for PA2\u2010Vb in the vascular system.\n                  <\/jats:p>","DOI":"10.1016\/j.febslet.2014.10.032","type":"journal-article","created":{"date-parts":[[2014,11,4]],"date-time":"2014-11-04T07:05:59Z","timestamp":1415084759000},"page":"4604-4612","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Crystal structure of phospholipase PA2\u2010Vb, a protease\u2010activated receptor agonist from the\n                    <i>Trimeresurus stejnegeri<\/i>\n                    snake 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