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Crystal Structure of Basic Phospholipase A2 from Agkistrodon Halys Pallas Crystal

机译:Agkistrodon Halys Pallas晶体的碱性磷脂酶A2的晶体结构

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摘要

Phospholipase A2 (PLA2, EC 3.1.1.4) specifically catalyzes the hydrolysis of the C-2 ester bond of 3-sn-phosphoglycerides to produce lysophosphatidylcholine and fatty acids in a calcium-dependent reaction. In this communication, we describe the structures of the three crystal forms of the low molecular mass (14KD) basic phospholipase A2 (BPLA2) isolated from the venom of Agkistrodon halys Pallas. BPLA2 is a strong hemolytic toxin and one of the few PLA2 capable of hydrolyzing the phospholipids of E. coli membranes in the presence of a bactericidal /permeability-increasing protein (BPI) of neutrophils.
机译:磷脂酶A2(PLA2,EC 3.1.1.4)在钙依赖性反应中特异性催化3-sn-磷酸甘油酯的C-2酯键水解,生成溶血磷脂酰胆碱和脂肪酸。在本交流中,我们描述了从Agkistrodon halys Pallas毒液中分离出的低分子量(14KD)碱性磷脂酶A2(BPLA2)的三种晶体形式的结构。 BPLA2是一种强溶血毒素,是在嗜中性粒细胞的杀菌/通透性增强蛋白(BPI)存在下能够水解大肠杆菌膜磷脂的少数PLA2之一。

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  • 来源
  • 会议地点 Guilin(CN)
  • 作者单位

    National Laboratoiy of Biomacromolecules, Institute of Biophysics,Academia Sinica, Beijing 100101;

    National Laboratoiy of Biomacromolecules, Institute of Biophysics,Academia Sinica, Beijing 100101;

    Shanghai Institute of Biochemistry,Academia Sinica, Shanghai 200023, China;

    National Laboratoiy of Biomacromolecules, Institute of Biophysics,Academia Sinica, Beijing 100101;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 Q-55;
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