Grb10 SH2 Domain: Difference between revisions
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==Dimerization of the Grb10 SH2 Domain== | ==Dimerization of the Grb10 SH2 Domain== | ||
The crystal structure of Grb10 SH2 domain was an important step to understanding how this protein interacts with IGF1 receptors, and although the SH2 domain functions as an independent segment, it forms a dimer in physiological environments. The <scene name='Grb10_SH2_Domain/ | The crystal structure of Grb10 SH2 domain was an important step to understanding how this protein interacts with IGF1 receptors, and although the SH2 domain functions as an independent segment, it forms a dimer in physiological environments. The <scene name='Grb10_SH2_Domain/Best_interface/1'>protein interface</scene> exists due to non-covalent intermolecular forces between Phenylalanine515, Tyrosine516, and Asparganine519 of each independent monomer <ref name=Guan>PMID: 12551896 </ref>. The structure of Grb10 SH2 forms similar SH2 domains found in other proteins, which have an <scene name='Grb10_SH2_Domain/Alpha_helix/1'>alpha helix</scene> on the outsides with anti-parallel <scene name='Grb10_SH2_Domain/Beta_sheet/1'>beta sheets</scene>. | ||
<scene name='Grb10_SH2_Domain/Dimer_interface/2'>Zoom?</scene> | <scene name='Grb10_SH2_Domain/Dimer_interface/2'>Zoom?</scene> | ||
Revision as of 03:56, 8 November 2012
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Interaction Between Grb10 and E3 Ubiquitin Ligase NEDD4
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Crystal structure of the NEDD4 C2-GRB10 SH2 complex
