Sandbox reserved 919: Difference between revisions

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<scene name='58/580297/3dnm_cartoon_dotsribbon/1'>Hormone-sensitive lipases</scene> are generally well-conserved across species. HSL is composed of two main structural domains, consisting of a slightly variable N-terminus that is thought to contribute to numerous factors including activity, specificity, regioselectivity, thermophilicity, and thermostability. The second, highly conserved, domain of HSL is the C-terminal catalytic domain, which contains the [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad], viewed <scene name='58/580297/3dnm_triad_zoomedout/1'>here</scene>, a charge relay network that is characteristic of many hydrolases. Size-exclusion chromatography studies have shown that HSL has a ligand pocket that is approximately 16Å deep, suggesting that HSL primarily hydrolyzes shorter chained molecules. <ref name="Nam">PMID:19089974</ref>

The catalytic triad <scene name='58/580297/3dnm_triad_zoomedin/1'>situates itself</scene> toward the middle of HSL. The catalytic triad is composed of residues <scene name='58/580297/3dnm_ligandsite_triad_chains/4'>Ser157, Glu251, and His281</scene>. The Ser157 residue sits at a site deemed the "nucleophilic elbow," that models an approximate torsion of Φ = 60° and Ψ =-120°. This nucleophilic elbow is stabilized by a hydrogen bond between the proximal nitrogen and oxygen atoms of His281 and Glu251, respectively. This model also shows the strong nucleophilic character of Ser157, portraying the covalent binding to <scene name='58/580297/3dnm_ligandsite_triad_chains/3'>β-mercaptoethanol</scene>. Return to default view, <scene name='58/580297/3dnm_cartoon/3'>here</scene>.

~~<scene name='58/580297/3dnm_ligandsite_triad_chains/3'>TextToBeDisplayed</scene>~~

The catalytic triad <scene name='58/580297/3dnm_triad_zoomedin/1'>situates itself</scene> toward the middle of HSL. The catalytic triad is composed of residues <scene name='58/580297/3dnm_ligandsite_triad_chains/3'>Ser157, Glu251, and His281</scene>. The Ser157 residue sits at a site deemed the "nucleophilic elbow," that models an approximate torsion of Φ = 60° and Ψ =-120°. This nucleophilic elbow is stabilized by a hydrogen bond between the proximal nitrogen and oxygen atoms of His281 and Glu251, respectively. This model also shows the strong nucleophilic character of Ser157, portraying the covalent binding to <scene name='58/580297/~~3dnm_cartoon_ligand~~/2'>β-mercaptoethanol</scene>. Return to default view, <scene name='58/580297/3dnm_cartoon/3'>here</scene>.

Sandbox reserved 919: Difference between revisions

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 <scene name='58/580297/3dnm_cartoon_dotsribbon/1'>Hormone-sensitive lipases</scene> are generally well-conserved across species. HSL is composed of two main structural domains, consisting of a slightly variable N-terminus that is thought to contribute to numerous factors including activity, specificity, regioselectivity, thermophilicity, and thermostability. The second, highly conserved, domain of HSL is the C-terminal catalytic domain, which contains the [http://en.wikipedia.org/wiki/Catalytic_triad catalytic triad], viewed <scene name='58/580297/3dnm_triad_zoomedout/1'>here</scene>, a charge relay network that is characteristic of many hydrolases. Size-exclusion chromatography studies have shown that HSL has a ligand pocket that is approximately 16Å deep, suggesting that HSL primarily hydrolyzes shorter chained molecules. <ref name="Nam">PMID:19089974</ref>
+The catalytic triad <scene name='58/580297/3dnm_triad_zoomedin/1'>situates itself</scene> toward the middle of HSL. The catalytic triad is composed of residues <scene name='58/580297/3dnm_ligandsite_triad_chains/4'>Ser157, Glu251, and His281</scene>. The Ser157 residue sits at a site deemed the "nucleophilic elbow," that models an approximate torsion of Φ = 60° and Ψ =-120°. This nucleophilic elbow is stabilized by a hydrogen bond between the proximal nitrogen and oxygen atoms of His281 and Glu251, respectively. This model also shows the strong nucleophilic character of Ser157, portraying the covalent binding to <scene name='58/580297/3dnm_ligandsite_triad_chains/3'>β-mercaptoethanol</scene>. Return to default view, <scene name='58/580297/3dnm_cartoon/3'>here</scene>.
-<scene name='58/580297/3dnm_ligandsite_triad_chains/3'>TextToBeDisplayed</scene>
-The catalytic triad <scene name='58/580297/3dnm_triad_zoomedin/1'>situates itself</scene> toward the middle of HSL. The catalytic triad is composed of residues <scene name='58/580297/3dnm_ligandsite_triad_chains/3'>Ser157, Glu251, and His281</scene>. The Ser157 residue sits at a site deemed the "nucleophilic elbow," that models an approximate torsion of Φ = 60° and Ψ =-120°. This nucleophilic elbow is stabilized by a hydrogen bond between the proximal nitrogen and oxygen atoms of His281 and Glu251, respectively. This model also shows the strong nucleophilic character of Ser157, portraying the covalent binding to <scene name='58/580297/3dnm_cartoon_ligand/2'>β-mercaptoethanol</scene>. Return to default view, <scene name='58/580297/3dnm_cartoon/3'>here</scene>.