       Document 0606
 DOCN  M9640606
 TI    A mean field model of ligand-protein interactions: implications for the
       structural assessment of human immunodeficiency virus type 1 protease
       complexes and receptor-specific binding.
 DT    9604
 AU    Verkhivker GM; Rejto PA; Agouron Pharmaceuticals Inc., San Diego, CA
       92121, USA.
 SO    Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):60-4. Unique Identifier :
       AIDSLINE MED/96133877
 AB    We propose a general mean field model of ligand-protein interactions to
       determine the thermodynamic equilibrium of a system at finite
       temperature. The method is employed in structural assessments of two
       human immuno-deficiency virus type 1 protease complexes where the gross
       effects of protein flexibility are incorporated by utilizing a data base
       of crystal structures. Analysis of the energy spectra for these
       complexes has revealed that structural and thermo-dynamic aspects of
       molecular recognition can be rationalized on the basis of the extent of
       frustration in the binding energy landscape. In particular, the
       relationship between receptor-specific binding of these ligands to human
       immunodeficiency virus type 1 protease and a minimal frustration
       principle is analyzed.
 DE    Aspartic Proteinases/CHEMISTRY  HIV Protease/*CHEMISTRY  HIV Protease
       Inhibitors/*CHEMISTRY  HIV-1/*ENZYMOLOGY  Ligands
       Oligopeptides/*CHEMISTRY  *Protein Binding  Protein Conformation
       Temperature  Thermodynamics  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

