The active site of the homodimeric HIV-1 protease includes six amino acids
(triads AspThrGly found in each monomer) in amino acid positions 25 to 27 a
nd 25 ' to 27 '. Up to now, the role of Thr26 and Thr26 ', and Gly27 and Gl
y27 ', is unknown. It is hypothesized that strong hydrogen-bonding forces b
etween the Thr26 and Thr26 ' residues stabilize the conformational state of
the active site, and that the function of Gly27 and Gly27 ' is to accommod
ate and bind a substrate in a position in which the catalytic Asp25 and Asp
25 ' carboxylate groups can attack the amide moiety of a substrate. (C) 200
1 John Wiley & Sons, Inc.