Please use this identifier to cite or link to this item: https://doi.org/10.1111/j.1742-4658.2005.04547.x
Title: Structure and function comparison of Micropechis ikaheka snake venom phospholipase A2 isoenzymes
Authors: Lok, S.-M.
Gao, R. 
Rouault, M.
Lambeau, G.
Gopalakrishnakone, P.
Swaminathan, K. 
Keywords: Crystal structure
Group IB phospholipase A2
Micropechis ikaheka
Pharmacological determinant
Issue Date: Mar-2005
Citation: Lok, S.-M., Gao, R., Rouault, M., Lambeau, G., Gopalakrishnakone, P., Swaminathan, K. (2005-03). Structure and function comparison of Micropechis ikaheka snake venom phospholipase A2 isoenzymes. FEBS Journal 272 (5) : 1211-1220. ScholarBank@NUS Repository. https://doi.org/10.1111/j.1742-4658.2005.04547.x
Abstract: Comparison of the crystal structures of three Micropechis ikaheka phospholipase A2 isoenzymes (MiPLA2, MiPLA3 and MiPLA4, which exhibit different levels of pharmacological effects) shows that their C-terminus (residues 110-124) is the most variable. M-Type receptor binding affinity of the isoenzymes has also been investigated and MiPLA4 binds to the rabbit M-type receptor with high affinity. Examination of surface charges of the isoenzymes reveals a trend of increase in positive charges with potency. The isoenzymes are shown to oligomerize in a concentration-dependent manner in a semi-denaturing gel. The C-termini of the medium (MiPLA4) and highly potent (MiPLA2) isoenzyme molecules cluster together, forming a highly exposed area. A BLAST search using the sequence of the most potent MiPLA2 results in high similarity to Staphylococcus aureus clotting factor A and cadherin 11. This might explain the myotoxicity, anticoagulant and hemoglobinuria effects of MiPLA2s. © 2005 FEBS.
Source Title: FEBS Journal
URI: http://scholarbank.nus.edu.sg/handle/10635/112653
ISSN: 1742464X
DOI: 10.1111/j.1742-4658.2005.04547.x
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

15
checked on Aug 16, 2019

WEB OF SCIENCETM
Citations

15
checked on Aug 16, 2019

Page view(s)

53
checked on Aug 16, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.