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. Author manuscript; available in PMC: 2010 Sep 1.
Published in final edited form as: Chem Biol Drug Des. 2009 Sep;74(3):246–257. doi: 10.1111/j.1747-0285.2009.00855.x

Figure 1.

Figure 1

Crystal structure of part of domain IV of HER2 interacting with herceptin. Three important pockets (two electrostatic and one hydrophobic) in the interaction region are shown. Residues that form the hydrogen bonding and hydrophobic interaction in the binding pocket of HER2-herceptin are shown. Residues from herceptin are shown as red sticks and residues from HER2 protein domain IV are shown in blue. Amino acid residues from herceptin are labeled with a three letter code and residues from HER2 protein are labeled with a single letter amino acid code.