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Figure 2.
Fig. 2. Details of the interaction between GLFG and FxFG
cores and Ib442. Stereo views of GLFG (A, black) and FxFG (B,
red) cores show that each binds in the hydrophobic pocket
(yellow) formed between HEAT repeats 5 (light green) and 6
(light blue) by the side chains of Leu174, Thr175, Ile^178,
Glu214, Phe^217, and Ile^218. In addition to the hydrophobic
interaction, putative H-bonds are formed between the main chain
and Glu214. Thr175 forms a H-bond to the FxFG core but not to
the GLFG core. Surface views (D and E) illustrate the intimacy
of the contact between the repeat cores and Ib442. In contrast,
the contact between the GLFG peptide at site 2 involved a pocket
formed by two Ib442 chains (green and orange in C and F) and
neither Ib442 chain alone buried a significant amount of the
core, consistent with site 2 representing a crystallization
artifact and site 1 representing the true GLFG binding site. G,
although the conformation of GLFG and FxFG cores bound to Ib442
was different, they had a similar outline.
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