HIV-1 protease-inhibitor binding dynamics and thermodynamics

Computer simulations of HIV-1 protease-inhibitor binding dynamics and thermodynamics 

Theoretical Biochemistry - Processes and Properties of Biological Systems Theoretical and Computational Chemistry, Vol. 9 2001 Elsevier Science B.V. All rights reserved 

Department of Biological Sciences, Central Campus, University of Essex, Wivenhoe Park, Colchester, Essex, C04 3SQ, Email reync essex.ac.uk, URL http //www. essex. ac. uk/bcs/staff/reync/ 

The major structural characteristics of the GPCR family are the seven hydrophobic domains, 20-30 residues in length, which span the membrane as antiparallel a helices. The helices are intercormected by three intracellular ill, il2 ii3) and three extracellular loops ell, el2, el3 forming a seven-helix bundle in a simTar but not identical fashion to bacteriorhodopsin (bR). However, despite the common structural motif, bR has no sequence similarity to other GPCR sequences and does r ot bind and activate a G-protein. 

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