Sandbox reserved 919: Difference between revisions

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<scene name='58/580297/3dnm_cartoon_surface/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], 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>

<scene name='58/580297/3dnm_cartoon_surface/2'>TextToBeDisplayed</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], 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>

<scene name='58/580297/3dnm_triad_zoomedout/1'>TextToBeDisplayed</scene>

<scene name='58/580297/3dnm_triad_zoomedin/1'>TextToBeDisplayed</scene>

<scene name='58/580297/3dnm_ligandsite_triad_chains/1'>TextToBeDisplayed</scene>

<scene name='58/580297/3dnm_ligandsite_triad_chains/2'>TextToBeDisplayed</scene>

The <scene name='58/580297/3dnm_ligandsite_charge_relay/1'>catalytic triad</scene> is comprised of Ser157, Glu251, and His281. 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 Ser157 residue to be stabilized by the covalent binding of <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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 <StructureSection load='3DNM' size='350' frame='true' align='right' caption='Hormone-Sensitive Lipase from [[3dnm]]' scene='58/580297/3dnm_cartoon/2' >
-<scene name='58/580297/3dnm_cartoon_surface/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], 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>
+<scene name='58/580297/3dnm_cartoon_surface/2'>TextToBeDisplayed</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], 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>
 <scene name='58/580297/3dnm_triad_zoomedout/1'>TextToBeDisplayed</scene>
 <scene name='58/580297/3dnm_triad_zoomedin/1'>TextToBeDisplayed</scene>
-<scene name='58/580297/3dnm_ligandsite_triad_chains/1'>TextToBeDisplayed</scene>
+<scene name='58/580297/3dnm_ligandsite_triad_chains/2'>TextToBeDisplayed</scene>
 The <scene name='58/580297/3dnm_ligandsite_charge_relay/1'>catalytic triad</scene> is comprised of Ser157, Glu251, and His281. 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 Ser157 residue to be stabilized by the covalent binding of <scene name='58/580297/3dnm_cartoon_ligand/2'>β-mercaptoethanol</scene>. Return to default view, <scene name='58/580297/3dnm_cartoon/3'>here</scene>.