Keys to Lipid Selection in Fatty Acid Amide Hydrolase Catalysis: Structural Flexibility, Gating Residues and Multiple Binding Pockets

@inproceedings{Palermo2015KeysTL,
  title={Keys to Lipid Selection in Fatty Acid Amide Hydrolase Catalysis: Structural Flexibility, Gating Residues and Multiple Binding Pockets},
  author={Giulia Palermo and Inga Bauer and Pablo Campomanes and Andrea Cavalli and Andrea Armirotti and Stefania Girotto and Ursula Rothlisberger and Marco de Vivo},
  booktitle={PLoS Computational Biology},
  year={2015}
}
The fatty acid amide hydrolase (FAAH) regulates the endocannabinoid system cleaving primarily the lipid messenger anandamide. FAAH has been well characterized over the years and, importantly, it represents a promising drug target to treat several diseases, including inflammatory-related diseases and cancer. But its enzymatic mechanism for lipid selection to specifically hydrolyze anandamide, rather than similar bioactive lipids, remains elusive. Here, we clarify this mechanism in FAAH… CONTINUE READING
Related Discussions
This paper has been referenced on Twitter 4 times. VIEW TWEETS

References

Publications referenced by this paper.
Showing 1-10 of 76 references

Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling.

Chembiochem : a European journal of chemical biology • 2010
View 11 Excerpts
Highly Influenced

Structure and function of fatty acid amide hydrolase.

Annual review of biochemistry • 2005
View 7 Excerpts
Highly Influenced

Validation and use of the MM-PBSA approach for drug discovery.

Journal of medicinal chemistry • 2005
View 11 Excerpts
Highly Influenced

Fatty acid amide hydrolase substrate specificity.

Bioorganic & medicinal chemistry letters • 2000
View 6 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…