Figure 4.
Figure 4. Functional maps of HsTx1 and [Abu^19,Abu^34]-HsTx1
for Kv1.1 and Kv1.3 channels. These peptide functional maps were
deduced from docking simulation experiments using the 3D
structures of HsTx1 and [Abu^19,Abu^34]-HsTx1 and modeled
structures of the pore regions of mKv1.1 and mKv1.3 channels.
Interacting residues from the Kv channels are shown in red. I to
IV before channel residue numbering specifies one of the four
-subunits
forming the functional Kv channels. Color codes: yellow
(hydrophobic residues), light green (polar residues), and blue
(basic residues). Swiss-Prot accession codes used are P16388
(mKv1.1) and P16390 (mKv1.3). (A) Functional maps for HsTx1
(left) and [Abu^19,Abu^34]-HsTx1 (right) on Kv1.1. (B)
Functional maps for HsTx1 (left) and [Abu^19,Abu^34]-HsTx1
(right) on Kv1.3. The functional maps of both peptides involve
mainly their -sheet
faces.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2005,
61,
1010-1023)
copyright 2005.
-subunits
forming the functional Kv channels. Color codes: yellow
(hydrophobic residues), light green (polar residues), and blue
(basic residues). Swiss-Prot accession codes used are P16388
(mKv1.1) and P16390 (mKv1.3). (A) Functional maps for HsTx1
(left) and [Abu^19,Abu^34]-HsTx1 (right) on Kv1.1. (B)
Functional maps for HsTx1 (left) and [Abu^19,Abu^34]-HsTx1
(right) on Kv1.3. The functional maps of both peptides involve
mainly their 
-sheet
faces.