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">PMID: 7773779</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 (<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"/>

Sandbox Reserved 1124: Difference between revisions

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Revision as of 10:45, 30 January 2016 view source Camille Torlotin (talk \| contribs) 83 edits No edit summary ← Older edit		Revision as of 10:47, 30 January 2016 view source Albertine Serfaty (talk \| contribs) 60 edits No edit summary Newer edit →
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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">PMID: 7773779</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 (<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"/>		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"/>