Figure 2.
Fig. 2. A stereoview of the -carbon
trace of the crystalline App-D49 indicating the positions of
mutated residues. The view of the enzyme shown here is similar
to that used in previous publications to illustrate the location
of a co-crystallized transition-state^ analog (9, 17, 28). The
active site lies at the base of^ the central cavity formed from
the amino-terminal helix, residues 19-23, portions of the
calcium-binding loop, and the side chain of Lys-69 and is
indicated by the side chain of His-48 (in black). The plane of
the putative interfacial adsorption surface lies perpendicular
to the hydrophobic channel and incorporates residues surrounding
the external opening of the channel. In the present study,
specific lysine residues (Lys-7, Lys-10, Lys-11, Lys-16, Lys-54,
and Lys-69) were changed into glutamates and tyrosine^ (Lys-69)
in an effort to characterize the structural determinants of
interfacial adsorption.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(1997,
272,
3573-3582)
copyright 1997.
-carbon
trace of the crystalline App-D49 indicating the positions of
mutated residues. The view of the enzyme shown here is similar
to that used in previous publications to illustrate the location
of a co-crystallized transition-state^ analog (9, 17, 28). The
active site lies at the base of^ the central cavity formed from
the amino-terminal helix, residues 19-23, portions of the
calcium-binding loop, and the side chain of Lys-69 and is
indicated by the side chain of His-48 (in black). The plane of
the putative interfacial adsorption surface lies perpendicular
to the hydrophobic channel and incorporates residues surrounding
the external opening of the channel. In the present study,
specific lysine residues (Lys-7, Lys-10, Lys-11, Lys-16, Lys-54,
and Lys-69) were changed into glutamates and tyrosine^ (Lys-69)
in an effort to characterize the structural determinants of
interfacial adsorption.