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M9640606.TXT
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1996-03-04
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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).