3jr8

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Template:STRUCTURE 3jr8

Contents

Crystal Structure of BthTX-II (Asp49-PLA2 from Bothrops jararacussu snake venom) with calcium ions

Template:ABSTRACT PUBMED 20878713

Function

[PA2B2_BOTJR] Snake venom phospholipase A2 (PLA2) that shows a moderate enzymatic activity. It induces indirect hemolytic, anticoagulant, and cytotoxic activities. In vivo, it induces muscle necrosis, accompanied by polymorphonuclear cell infiltration, and edema in the mouse paw. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.[1] [2]

About this Structure

3jr8 is a 2 chain structure with sequence from Bothrops jararacussu. Full crystallographic information is available from OCA.

Reference

  • dos Santos JI, Cintra-Francischinelli M, Borges RJ, Fernandes CA, Pizzo P, Cintra AC, Braz AS, Soares AM, Fontes MR. Structural, functional, and bioinformatics studies reveal a new snake venom homologue phospholipase A(2) class. Proteins. 2011 Jan;79(1):61-78. doi: 10.1002/prot.22858. Epub 2010 Sep 27. PMID:20878713 doi:10.1002/prot.22858
  1. Pereira MF, Novello JC, Cintra AC, Giglio JR, Landucci ET, Oliveira B, Marangoni S. The amino acid sequence of bothropstoxin-II, an Asp-49 myotoxin from Bothrops jararacussu (Jararacucu) venom with low phospholipase A2 activity. J Protein Chem. 1998 May;17(4):381-6. PMID:9619591
  2. Andriao-Escarso SH, Soares AM, Rodrigues VM, Angulo Y, Diaz C, Lomonte B, Gutierrez JM, Giglio JR. Myotoxic phospholipases A(2) in bothrops snake venoms: effect of chemical modifications on the enzymatic and pharmacological properties of bothropstoxins from Bothrops jararacussu. Biochimie. 2000 Aug;82(8):755-63. PMID:11018293

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