Sphingosine kinase: Difference between revisions
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The <scene name='91/910628/Sphk1_surface/4'>catalytic site</scene> (used in converting sphingosine to S1P-see below in "Sphingolipids" section for more details) is in a <scene name='91/910628/Sphk1_hydrophobic_pocket/1'>'''hydrophobic''' cleft</scene>, located between the two domains. <ref name="wang">PMID:23602659</ref> This hydrophobic cleft is an '''ideal binding pocket''' for a '''hydrophobic lipid''', like sphingosine (an '''18-carbon''' amino alcohol with an '''unsaturated''' '''hydrocarbon''' chain). <ref name="wang">PMID:23602659</ref> The binding of sphingosine to the SphK1 hydrophobic "pocket" is mediated by both the anchoring of the <scene name='91/910628/Sphingosine_element_label/2'>hydrophilic (polar) headgroup</scene> of sphingosine to the protein surface and the presence of the hydrophobic alkyl chain in the interior of the protein. <ref name="wang">PMID:23602659</ref> The 2-amino-1,3-diol moiety of the sphingosine head group is situated at the cleft between the two domains, allowing for '''hydrogen-bond interactions''' ('''Figure 1''') with <scene name='91/910628/Amino_acid_interactions/4'>Asp81 through the 1-hydroxyl and with Asp178 through the 3-hydroxyl</scene>, which also forms a water-mediated hydrogen bond with Ser168. Sphingosine's long acyl chain is buried in the hydrophobic pocket ("tunnel shaped"), lined by side chains of mostly <scene name='91/910628/Amino_acid_interactions/6'>non-polar amino acid residues</scene> (i.e., Phe173, Ile174, Val177, Phe192, Thr196, Leu299, Leu302, Phe303, Met306, His311, Leu319, Phe288, Val290, Leu259, Leu261, Ala170, Met272, and Ala274). <ref name="wang">PMID:23602659</ref> | The <scene name='91/910628/Sphk1_surface/4'>catalytic site</scene> (used in converting sphingosine to S1P-see below in "Sphingolipids" section for more details) is in a <scene name='91/910628/Sphk1_hydrophobic_pocket/1'>'''hydrophobic''' cleft</scene>, located between the two domains. <ref name="wang">PMID:23602659</ref> This hydrophobic cleft is an '''ideal binding pocket''' for a '''hydrophobic lipid''', like sphingosine (an '''18-carbon''' amino alcohol with an '''unsaturated''' '''hydrocarbon''' chain). <ref name="wang">PMID:23602659</ref> The binding of sphingosine to the SphK1 hydrophobic "pocket" is mediated by both the anchoring of the <scene name='91/910628/Sphingosine_element_label/2'>hydrophilic (polar) headgroup</scene> of sphingosine to the protein surface and the presence of the hydrophobic alkyl chain in the interior of the protein. <ref name="wang">PMID:23602659</ref> The 2-amino-1,3-diol moiety of the sphingosine head group is situated at the cleft between the two domains, allowing for '''hydrogen-bond interactions''' ('''Figure 1''') with <scene name='91/910628/Amino_acid_interactions/4'>Asp81 through the 1-hydroxyl and with Asp178 through the 3-hydroxyl</scene>, which also forms a water-mediated hydrogen bond with Ser168. Sphingosine's long acyl chain is buried in the hydrophobic pocket ("tunnel shaped"), lined by side chains of mostly <scene name='91/910628/Amino_acid_interactions/6'>non-polar amino acid residues</scene> (i.e., Phe173, Ile174, Val177, Phe192, Thr196, Leu299, Leu302, Phe303, Met306, His311, Leu319, Phe288, Val290, Leu259, Leu261, Ala170, Met272, and Ala274). <ref name="wang">PMID:23602659</ref> | ||
[[Image:SphK1 Sequence and Structure Conservation Small.jpeg|300px|right|thumb|'''Figure 2'''. SphK1 Sequence Conservation Structure with Conservation Table in Figure 4]] | [[Image:SphK1 Sequence and Structure Conservation Small.jpeg|300px|right|thumb|'''Figure 2'''. SphK1 Sequence Conservation Structure with Conservation Table in Figure 4]] | ||
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== References == | == References == | ||
<references/> | <references/> | ||
</StructureSection> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||