Sandbox Reserved 1124: Difference between revisions
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<scene name='71/719865/Sh3_domain_1/1'>The N-terminal SH3 domain</scene> plays the main role in the interaction with the SOS protein. It binds a proline-rich motif PxxP of the C-Terminal domain of SOS<ref name="a">DOI:10.1038/nsb1294-898</ref> and this binding region in SOS has the shape of a Polyprolin II helix. | <scene name='71/719865/Sh3_domain_1/1'>The N-terminal SH3 domain</scene> plays the main role in the interaction with the SOS protein. It binds a proline-rich motif PxxP of the C-Terminal domain of SOS<ref name="a">DOI:10.1038/nsb1294-898</ref> and this binding region in SOS has the shape of a Polyprolin II helix. | ||
The N-terminal SH3 domain encompasses two three-stranded antiparallel β-sheets, one strand crosses the two sheets. This confers a barrel-like structure upon the domain. The first sheet contains the 3 following strands: S1 (Glu2-Ala5), S2 (Ile24-Lys26) and S6 (Ile53-Met55). The second sheet contains the strands S3 (Val27-Asn29), S4 (Trp36-Leu41) and S5 (Asp45-Ile48). The structure of this SH3 domain is stabilized by a high number of hydrophobic residues, which form the centre of the protein.<ref name="a"/> | The N-terminal SH3 domain encompasses two three-stranded antiparallel β-sheets, one strand crosses the two sheets. This confers a barrel-like structure upon the domain. The first sheet contains the 3 following strands: S1 (<scene name='71/719865/Glu2-ala5/1'>Glu2-Ala5</scene>), S2 (<scene name='71/719865/Ile24-lys26/1'>Ile24-Lys26</scene>) and S6 (<scene name='71/719865/Ile53-met55/1'>Ile53-Met55</scene>). The second sheet contains the strands S3 (<scene name='71/719865/Val27-asn29/1'>Val27-Asn29</scene>), S4 (<scene name='71/719865/Trp36-leu41/1'>Trp36-Leu41</scene>) and S5 (<scene name='71/719865/Asp45-ile48/1'>Asp45-Ile48</scene>). The structure of this SH3 domain is stabilized by a high number of hydrophobic residues, which form the centre of the protein.<ref name="a"/> | ||
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<scene name='71/719865/C-terminal_sh3_domains/1'>The C-terminal SH3 domain</scene> goes from the amino acid 156 to 215. The role of this domain is little known. But it has been shown that, for a stable complex formation, the | <scene name='71/719865/C-terminal_sh3_domains/1'>The C-terminal SH3 domain</scene> goes from the amino acid 156 to 215. The role of this domain is little known. But it has been shown that, for a stable complex formation, the C-Terminal SH3 domain has to recognize a 13 residues sequence with the following motif: P-x-x-x-R-x-x-K-P. Sos contains this sequence, as well as Gab1, which also binds to Grb2. The interaction of Grb2 with Gab1 has been demonstrated with precipitation experiments. ref | ||
In the Ras pathway, the Ct SH3 domain improves the overall stability of the Grb2-SOS complex.<ref >DOI: http://dx.doi.org/10.1016/1074-5521(95)90080-2</ref> | In the Ras pathway, the Ct SH3 domain improves the overall stability of the Grb2-SOS complex.<ref >DOI: http://dx.doi.org/10.1016/1074-5521(95)90080-2</ref> | ||
