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
N-Myristoyltransferase (NMT) is a potential drug target in Leishmania parasites. Scaffold-hopping from published inhibitors yielded the serendipitous discovery of a chemotype selective for Leishmania donovani NMT; development led to high affinity inhibitors with excellent ligand efficiency. The binding mode was characterised by crystallography and provides a structural rationale for selectivity.
Discovery of high affinity inhibitors of -myristoyltransferase.,Rackham MD, Yu Z, Brannigan JA, Heal WP, Paape D, Barker KV, Wilkinson AJ, Smith DF, Leatherbarrow RJ, Tate EW Medchemcomm. 2015 Oct 8;6(10):1761-1766. Epub 2015 Aug 19. PMID:26962429[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rackham MD, Yu Z, Brannigan JA, Heal WP, Paape D, Barker KV, Wilkinson AJ, Smith DF, Leatherbarrow RJ, Tate EW. Discovery of high affinity inhibitors of -myristoyltransferase. Medchemcomm. 2015 Oct 8;6(10):1761-1766. Epub 2015 Aug 19. PMID:26962429 doi:http://dx.doi.org/10.1039/c5md00241a
