Grb10 SH2 Domain: Difference between revisions

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==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/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>.

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'>dimer interface</scene> exists due to the middle hydrophobic Phe515 and uncharged Thr504 (labeled blue) residues packed to the its equivalent counter parter on the other protomer, designated as Phe515' and Thr504' (labeled red); Gln511 (blue) forms a hydrogen bond to the backbone of Asp514' (red) while the side chain of Asn519 forms two hydrogen bonds to the backbone of Lys505'. <ref name=Guan>PMID: 12551896 </ref>. The interface ends with Leu518 and Phe-496' via hydrophobic interactions. <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>.

Grb10 SH2 Domain: Difference between revisions

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@@ Line 7: / Line 7: @@
 ==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/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>.
+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'>dimer interface</scene> exists due to the middle hydrophobic Phe515 and uncharged Thr504 (labeled blue) residues packed to the its equivalent counter parter on the other protomer, designated as Phe515' and Thr504' (labeled red); Gln511 (blue) forms a hydrogen bond to the backbone of Asp514' (red) while the side chain of Asn519 forms two hydrogen bonds to the backbone of Lys505'. <ref name=Guan>PMID: 12551896 </ref>.  The interface ends with Leu518 and Phe-496' via hydrophobic interactions. <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>