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Crystallization and preliminary X‐ray diffraction analysis of a myotoxic Lys49‐PLA 2 from Bothrops jararacussu venom complexed with p ‐bromophenacyl bromide
Author(s) -
MarchiSalvador D. P.,
Fernandes C. A. H.,
Amui S. F.,
Soares A. M.,
Fontes M. R. M.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910601801x
Subject(s) - bothrops , snake venom , bromide , venom , chemistry , active site , catalysis , biochemistry , organic chemistry
For the first time, a non‐catalytic and myotoxic Lys49‐PLA 2 (BthTX‐I from Bothrops jararacussu venom) has been crystallized with BPB inhibitor. X‐ray diffraction data were collected and electron‐density calculations showed that the ligand is bound to the His48 residue. BthTX‐I with His48 chemically modified by BPB shows strongly reduced myotoxic and cytotoxic activities. This suggests a biological correlation between the modification of His48, which is associated with catalytic activity of PLA 2 s, and other toxicological activities of Lys49‐PLA 2 s.

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