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. 2008 Sep 5;4(9):e1000177. doi: 10.1371/journal.pgen.1000177

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This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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Structural models of mouse wild type (A) and msp1-mutant (B) ERBB3 extracellular domains in the “closed” conformation. Negatively charged residues are shown in red, while positively charged residues are marked in blue. Protein domains I, II, III, and IV are labeled in yellow. The region of the msp1 mutation (yellow square) is located in domain II. C and D show close-up views of the regions denoted by the yellow squares in panels A and B. The msp1 mutation results in the loss of negative charge on the surface of the molecule. The bulky, negatively charged aspartic acid in the wild type protein is shown in red in panel C. This aspartic acid was replaced by glycine (a small, non-polar amino acid), shown in yellow in panel D.