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. 2015 Nov 5;2:15040. doi: 10.1038/hgv.2015.40

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Copyright © 2015 The Japan Society of Human Genetics

This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/

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Graphical representation of RASA1 Ras-Gap domain and Ras-p21 crystal structure detailing the impact of the identified p.E1015* (c.3043G>T) mutation. The surface of RASA1 Ras-Gap domain (residues 718–1037) surface is colored based on the Kyte–Doolittle hydrophobicity scale (hydrophobic regions in purple and hydrophilic areas in turquoise) and the Ras-p21 is in shown with gray surface. The p.E1015* variant would remove the C-terminal helix (orange) and would act to destabilize the GTPase-activating protein (GAP) domain by exposing the hydrophobic region to solvent. Images generated with chimera.¹⁴