Journal
MARINE DRUGS
Volume 11, Issue 6, Pages 1866-1877Publisher
MDPI
DOI: 10.3390/md11061866
Keywords
okadaic acid; protein phosphatase; nuclear magnetic resonance; scanning tunneling microscopy
Categories
Funding
- EU [KBBE-3-245137, FP7-REGPOT-2012-CT2012-316137]
- Spanish National Research Projects [SAF2011-28883-C03-01, CTQ2011-24784]
Ask authors/readers for more resources
Okadaic acid (OA) has been an invaluable pharmacological tool in the study of cellular signaling. The great affinity of this polyether for its targets together with its high specificity to inhibit certain protein phosphatases enables the differential study of these proteins. Crystallographic structures of protein phosphatases in complex with OA show a 1: 1 protein to toxin ratio. Nevertheless, it has been found that OA is able to self-associate under certain conditions although very little is known about the importance of this phenomenon. Here we review the available knowledge on the latter topic and we report on the existence of an unusual self-associated tetrameric form. The structure of these oligomers is proposed based on spectroscopic data and molecular modeling calculations.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available