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' > | |||
==Introduction to hormone-sensitive lipase== | ==Introduction to hormone-sensitive lipase== | ||
[[Image:HPL_firstimage.png|300 px|left|thumb|Hormone-Sensitive Lipase from [[3dnm]]. Alpha helices and beta sheets are shown in red and yellow, respectively.]] | [[Image:HPL_firstimage.png|300 px|left|thumb|Hormone-Sensitive Lipase from [[3dnm]]. Alpha helices and beta sheets are shown in red and yellow, respectively.]] | ||
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==Structure of hormone-sensitive lipase== | ==Structure of hormone-sensitive lipase== | ||
<scene name='58/580297/3dnm_cartoon_dotsribbon/1'>Hormone-sensitive lipases</scene> are generally well-conserved across domains, including prokaryotes, showing 29, 26, and 22% residue overlap in [http://en.wikipedia.org/wiki/Alicyclobacillus ''Alicyclobacillus acidocaldarius''], [http://en.wikipedia.org/wiki/Archaeoglobus ''Archaeoglobus fulgidus''], and [http://en.wikipedia.org/wiki/Bacillus_subtilis ''Bacillus subtilis''], respectively. <ref name="Nam">PMID:19089974</ref> HSL is composed of two main structural domains, consisting of a slightly variable N-terminus (shown in blue in the <scene name='58/580297/3dnm_cartoon/3'>default view</scene>) that is thought to contribute to numerous factors including activity, specificity, regioselectivity, thermophilicity, and thermostability. <ref name="Nam">PMID:19089974</ref> Research speculates that the N-terminal domain, consisting of about 300 residues, mediates protein-protein interactions, and possibly subsequent lipid binding. <ref name= "Yeaman">PMID:14725507</ref> The second domain of HSL is the C-terminal catalytic domain (colors other than blue), which contains serine residue phosphorylation sites as well as 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, such as [http://proteopedia.org/wiki/index.php/Chymotrypsin chymotrypsin]. <ref name= "Yeaman">PMID:14725507</ref> With respect to sequence conservation across species, it has been shown that the catalytic domain, including the triad, is conserved across domains, but the domain containing the N-terminus shows little conservation. <ref name="Nam">PMID:19089974</ref> Size-exclusion chromatography studies have shown that HSL has a <scene name='58/580297/3dnm_cartoon_surface/4'>ligand pocket</scene> 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_dotsribbon/1'>Hormone-sensitive lipases</scene> are generally well-conserved across domains, including prokaryotes, showing 29, 26, and 22% residue overlap in [http://en.wikipedia.org/wiki/Alicyclobacillus ''Alicyclobacillus acidocaldarius''], [http://en.wikipedia.org/wiki/Archaeoglobus ''Archaeoglobus fulgidus''], and [http://en.wikipedia.org/wiki/Bacillus_subtilis ''Bacillus subtilis''], respectively. <ref name="Nam">PMID:19089974</ref> HSL is composed of two main structural domains, consisting of a slightly variable N-terminus (shown in blue in the <scene name='58/580297/3dnm_cartoon/3'>default view</scene>) that is thought to contribute to numerous factors including activity, specificity, regioselectivity, thermophilicity, and thermostability. <ref name="Nam">PMID:19089974</ref> Research speculates that the N-terminal domain, consisting of about 300 residues, mediates protein-protein interactions, and possibly subsequent lipid binding. <ref name= "Yeaman">PMID:14725507</ref> The second domain of HSL is the C-terminal catalytic domain (colors other than blue), which contains serine residue phosphorylation sites as well as 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, such as [http://proteopedia.org/wiki/index.php/Chymotrypsin chymotrypsin]. <ref name= "Yeaman">PMID:14725507</ref> With respect to sequence conservation across species, it has been shown that the catalytic domain, including the triad, is conserved across domains, but the domain containing the N-terminus shows little conservation. <ref name="Nam">PMID:19089974</ref> Size-exclusion chromatography studies have shown that HSL has a <scene name='58/580297/3dnm_cartoon_surface/4'>ligand pocket</scene> that is approximately 16Å deep, suggesting that HSL primarily hydrolyzes shorter chained molecules. <ref name="Nam">PMID:19089974</ref> | ||
