Grb10 SH2 Domain: Difference between revisions
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Grb10 has now been shown to not only inhibit insulin receptors and IGF1R kinase activity, but also interacts via its SH2 domain with the C2 domain of E3 ubiquitin ligase NEDD4 facilitating ubiquitation of IGF1R <ref>PMID: 20980250</ref>. It is hypothesized that the Grb10 SH2 interaction with the E3 domain of NEDD4 may allow NEDD4 to come in close proximity to IGF1R promoting degradation.<ref>PMID: 20980250</ref> | Grb10 has now been shown to not only inhibit insulin receptors and IGF1R kinase activity, but also interacts via its SH2 domain with the C2 domain of E3 ubiquitin ligase NEDD4 facilitating ubiquitation of IGF1R <ref>PMID: 20980250</ref>. It is hypothesized that the Grb10 SH2 interaction with the E3 domain of NEDD4 may allow NEDD4 to come in close proximity to IGF1R promoting degradation.<ref>PMID: 20980250</ref> | ||
====There are 3 interfaces at which Nedd4 C2 and Grb10 SH2 interact:=== | ====There are 3 interfaces at which Nedd4 C2 and Grb10 SH2 interact:==== | ||
<scene name='Grb10_SH2_Domain/Interface_i/1'>Interface I</scene> is the largest of the 3 interfaces between Grb10 SH2 and NEDD4 C2 domains. There are 8 hydrogen bonds formed at this interface, with the least important H bonds formed between <scene name='Grb10_SH2_Domain/Interface_i/2'>ASN519 and LEU177</scene>, for disruption between these two residues with an induced mutation did not inhibit Grb10 SH2 and NEDD4 C2 to complex. <ref>PMID: 20980250</ref> | <scene name='Grb10_SH2_Domain/Interface_i/1'>Interface I</scene> is the largest of the 3 interfaces between Grb10 SH2 and NEDD4 C2 domains. There are 8 hydrogen bonds formed at this interface, with the least important H bonds formed between <scene name='Grb10_SH2_Domain/Interface_i/2'>ASN519 and LEU177</scene>, for disruption between these two residues with an induced mutation did not inhibit Grb10 SH2 and NEDD4 C2 to complex. <ref>PMID: 20980250</ref> | ||
<scene name='Grb10_SH2_Domain/Interface_ii/1'>Interface II</scene>, the smallest of the 3, is composed of residues 429-434 of Grb10 SH2 interacting with residues 112-114 of NEDD4 C2; disruption of this interaction does not disrupt the SH2-C2 domain complex. <ref>PMID: 20980250</ref> | |||
<scene name='Grb10_SH2_Domain/Interface_iii/1'>Interface III</scene> is made of NEDD4 C2's proline rich C terminus which complexes with Grb10 H2 N-terminal (residues 431-440) | |||
<scene name='Grb10_SH2_Domain/Interface_iii/1'> | |||
<scene name='Grb10_SH2_Domain/Interface_iii_hbond/1'>TextToBeDisplayed</scene> | <scene name='Grb10_SH2_Domain/Interface_iii_hbond/1'>TextToBeDisplayed</scene> | ||
