Structural highlights
Function
[Q4Q5S8_LEIMA] Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins (By similarity).
Publication Abstract from PubMed
Inhibitors of Leishmania NMT, a potential target for the treatment of leishmaniasis, obtained from a high-throughput screen were resynthesized to validate activity. Crystal structures bound to Leishmania major NMT were obtained and the active diastereoisomer of one of the inhibitors was identified. Based on structural insights, enzyme inhibition was increased 40-fold through hybridization of two distinct binding modes, resulting in novel, highly potent Leishmania donovani NMT inhibitors with good selectivity over the human enzyme.
Structure-Based Design of Potent and Selective Leishmania N-Myristoyltransferase Inhibitors.,Hutton JA, Goncalves V, Brannigan JA, Paape D, Wright MH, Waugh TM, Roberts SM, Bell AS, Wilkinson AJ, Smith DF, Leatherbarrow RJ, Tate EW J Med Chem. 2014 Sep 19. PMID:25238611[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hutton JA, Goncalves V, Brannigan JA, Paape D, Wright MH, Waugh TM, Roberts SM, Bell AS, Wilkinson AJ, Smith DF, Leatherbarrow RJ, Tate EW. Structure-Based Design of Potent and Selective Leishmania N-Myristoyltransferase Inhibitors. J Med Chem. 2014 Sep 19. PMID:25238611 doi:http://dx.doi.org/10.1021/jm5011397
