|
Figure 5.
Fig. 5. The structure of a unique hydrophobic pocket found in
the F–S cavity of AAL. (a) Structural alignment of AAL (main
chains in green and side chains in magenta) and galectin-1
(blue; PDB code 1LSA). It shows a structurally homologous cavity
between the F and S β-sheet layers in which a functionally
important hydrophobic pocket is identified in galectin-1. (b)
The hydrophobic pocket resided in the F–S cavity of AAL, which
consists of two hydrophobic residue clusters, LLFI (Leu33,
Leu35, Phe93, and Ile144; in magenta) and FLV (F28, Leu47, and
Val102; in cyan). (c) The unique LLFI cluster adopted an
integrated structural organization.
|
