Document 0048
 DOCN  M9460048
 TI    An alternate-subsite-coupled model for predicting HIV protease cleavage
       sites in proteins.
 DT    9404
 AU    Zhang CT; Chou KC; Department of Physics, Tianjin University, China.
 SO    Protein Eng. 1994 Jan;7(1):65-73. Unique Identifier : AIDSLINE
       MED/94188353
 AB    A 2-4-6 subsite-coupled model is proposed to predict the cleavability of
       peptide sequences by HIV protease. For an enzyme with eight extended
       specificity subsites, such as HIV protease, the coupling effects of the
       second subsite with the fourth one and the fourth with the sixth subsite
       are much more important than those of the others. Accordingly, in
       establishing a model for predicting whether a given peptide can be
       cleaved by HIV protease, the 2-4-6 subsite-coupled effect must be
       incorporated. The model leads to an algorithm for predicting
       protease-susceptible sites from primary structure. The high rate of
       correct prediction for both HIV-1 and HIV-2 proteases has borne out that
       this kind of alternation-coupled mechanism does exist along the extended
       subsites of HIV protease. The principle of the new method can be used
       for analyzing the specificity of any multisubsite enzyme. In particular,
       the new method can serve as a supplementary means for finding effective
       inhibitors of HIV protease, which is one of the targets in designing
       potential drugs for AIDS therapy.
 DE    *Algorithms  Amino Acid Sequence  Comparative Study  Hydrolysis  HIV
       Protease/*METABOLISM  HIV-1/*ENZYMOLOGY  HIV-2/*ENZYMOLOGY  *Models,
       Chemical  Models, Molecular  Molecular Sequence Data  Monte Carlo Method
       Oligopeptides/*CHEMISTRY  Substrate Specificity  JOURNAL ARTICLE

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