Abstract:
:DOCK and Affinity studies were carried out to study the binding of D- and L-penicillamine to the transactivator protein (tat) of human immunodeficiency virus type 1 (HIV-1). These studies reveal a selective binding of D-penicillamine to the cysteine-rich region covering amino acid residues 20-38 of the tat protein. A careful analysis of the components of the binding energy of the D- and L-isomers reveals that the D-isomer has a more favorable van der Waals interaction resulting from an optimal placement of the dimethylthiomethyl side chain in the binding site. This observation matches the experimental data that D-penicillamine is a more potent inhibitor of tat-mediated transactivation than the L-isomer. The docking and experimental data offer an interesting approach to design structural molecules with potential application to block signal functions of the tat protein in HIV-1 pathogenesis.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Demirhan I,Kanyalkar M,Chandra A,Doerr HW,Coutinho E,Loewer J,Saran A,Chandra Pdoi
10.1016/s0014-5793(02)02468-7keywords:
subject
Has Abstractpub_date
2002-04-10 00:00:00pages
43-6issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302024687journal_volume
516pub_type
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