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Figure 5.
Figure 5. (a) The front view of the BmTx3B-Kca1.1 channel
complex generated by MOLMOL. The residues, Lys28 and Arg35,
which have formed hydrogen bonds with the residues of the
channel, are marked. (b) The top view of the BmTx3B-Kca1.1
channel complex generated by the program WebLab ViewerPro 4.0.
The Kca1.1 channel is represented as a molecular surface colored
by electrostatic potential, and BmTx3B as a green tube
structure. (c and d) Interaction interfaces of BmTx3B with
Kca1.1. (right) and Kv1.3 (left). The key interactions pairs are
indicated with black lines, while, for clarity, the interactions
between Lys28 of BmTx3B and Tyr290 (I-IV) of the Kca1.1 channel
and Tyr395 (I-IV) of the Kv1.3 channel are not shown. Blue,
yellow, green, white, and gray surfaces represent basic,
sulfur-containing, polar, nonpolar, and aromatic residues,
respectively. The red quadrate lines highlight the peptide
residues involved in  -
or
hydrophobic core interactions. (e) Aromatic clusters in the
complex of BmTx3B (blue) and Kca1.1 channel (green). The
residues predicted to form the -
stacking
clusters are shown as red line models.
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