1ha2: Difference between revisions

==Overview==

Human serum albumin (HSA) is an abundant transport protein found in plasma, that binds a wide variety of drugs in two primary binding sites (I and II), and can have a significant impact on their pharmacokinetics. We have, determined the crystal structures at 2.5 A-resolution of HSA-myristate, complexed with the R-(+) and S-(-) enantiomers of warfarin, a widely used, anticoagulant that binds to the protein with high affinity. The structures, confirm that warfarin binds to drug site I (in subdomain IIA) in the, presence of fatty acids and reveal the molecular details of the, protein-drug interaction. The two enantiomers of warfarin adopt very, similar conformations when bound to the protein and make many of the same, specific contacts with amino acid side chains at the binding site, thus, accounting for the relative lack of stereospecificity of the HSA-warfarin, interaction. The conformation of the warfarin binding pocket is, significantly altered upon binding of fatty acids, and this can explain, the observed enhancement of warfarin binding to HSA at low levels of fatty, acid.

==About this Structure==

[[Category: serum protein]]