Figure 5.
Figure 5. Destabilization of the SH3 fold by the L180
mutations. (Left) Sructure of the wild-type nephrocystin SH3.
The side-chains of E156, L180, and K193 are indicated. (Right)
Model of the mutant L180P structure. The diverging type II -turn,
which folds independently in solution is highligthed in yellow.
After the MD simulation, the major structural change was the
movement of E156 and K193 side-chains, the terminal atoms of
which come in Van der Waals contact over the pyrrolidine ring of
P180 (right). This also induced a partial disruption of the
underlying -sheet
structure.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2005,
59,
347-355)
copyright 2005.
-turn,
which folds independently in solution is highligthed in yellow.
After the MD simulation, the major structural change was the
movement of E156 and K193 side-chains, the terminal atoms of
which come in Van der Waals contact over the pyrrolidine ring of
P180 (right). This also induced a partial disruption of the
underlying