Title : Structural and thermodynamic basis of the inhibition of Leishmania major farnesyl diphosphate synthase by nitrogen-containing bisphosphonates.

Pub. Date : 2014 Mar

PMID : 24598749






3 Functional Relationships(s)
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1 Here, the X-ray crystallographic structures of complexes of FPPS from Leishmania major (the causative agent of cutaneous leishmaniasis) with three bisphosphonates determined at resolutions of 1.8, 1.9 and 2.3 A are reported. Diphosphonates farnesyl diphosphate synthase Homo sapiens
2 Comparison of the structures of L. major FPPS (LmFPPS) and human FPPS provides new information for the design of bisphosphonates that will be more specific for inhibition of LmFPPS. Diphosphonates farnesyl diphosphate synthase Homo sapiens
3 Comparison of the structures of L. major FPPS (LmFPPS) and human FPPS provides new information for the design of bisphosphonates that will be more specific for inhibition of LmFPPS. Diphosphonates farnesyl diphosphate synthase Homo sapiens