4C7I

Leismania major N-myristoyltransferase in complex with a peptidomimetic (-OH) molecule

Summary for 4C7I

• Entry DOI: 10.2210/pdb4c7i/pdb
• Related: 4C68 4C7H
• Descriptor: GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE, TETRADECANOYL-COA, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: transferase, myristoylation
• Biological source: LEISHMANIA MAJOR
• Total number of polymer chains: 1
• Total formula weight: 49181.32

Authors

Olaleye, T.O.,Brannigan, J.A.,Goncalves, V.,Roberts, S.M.,Leatherbarrow, R.J.,Wilkinson, A.J.,Tate, E.W. (deposition date: 2013-09-20, release date: 2014-09-24, Last modification date: 2024-05-08)

Primary citation

Olaleye, T.O.,Brannigan, J.A.,Roberts, S.M.,Leatherbarrow, R.J.,Wilkinson, A.J.,Tate, E.W.
Peptidomimetic Inhibitors of N-Myristoyltransferase from Human Malaria and Leishmaniasis Parasites.
Org.Biomol.Chem., 12:8132-, 2014

PubMed Abstract: N-Myristoyltransferase (NMT) has been shown to be essential in Leishmania and subsequently validated as a drug target in Plasmodium. Herein, we discuss the use of antifungal NMT inhibitors as a basis for inhibitor development resulting in the first sub-micromolar peptidomimetic inhibitors of Plasmodium and Leishmania NMTs. High-resolution structures of these inhibitors with Plasmodium and Leishmania NMTs permit a comparative analysis of binding modes, and provide the first crystal structure evidence for a ternary NMT-Coenzyme A/myristoylated peptide product complex.

PubMed: 25230674
DOI: 10.1039/C4OB01669F

Experimental method

X-RAY DIFFRACTION (1.3 Å)