User:Maggie Stopa/Sandbox 1: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Maggie Stopa (talk | contribs) No edit summary |
Maggie Stopa (talk | contribs) No edit summary |
||
| Line 7: | Line 7: | ||
==Structural Overview== | ==Structural Overview== | ||
===LPL=== | ===LPL=== | ||
<scene name='87/877513/Original_scene/1'>LPL</scene> is assumed to only be active as a <scene name='87/877513/Lpl_dimer/4'>homodimer</scene>, however, previous studies have argued that the lipase can be active in its <scene name='87/877513/Original_scene/1'>monomeric form</scene>. (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6442593/) The N-terminal domain of lipoprotein lipase is known to consist of an alpha/beta hydrolase domain, which is composed of six alpha helices and ten beta-strands. This domain creates an <scene name='87/877513/Alpha-beta_hydrolase_domain_1/3'>alpha beta hydrolase fold</scene>. | <scene name='87/877513/Original_scene/1'>LPL</scene> is assumed to only be active as a <scene name='87/877513/Lpl_dimer/4'>homodimer</scene>, however, previous studies have argued that the lipase can be active in its <scene name='87/877513/Original_scene/1'>monomeric form</scene>. (https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6442593/) The N-terminal domain of lipoprotein lipase is known to consist of an alpha/beta hydrolase domain, which is composed of six alpha helices and ten beta-strands. This domain creates an <scene name='87/877513/Alpha-beta_hydrolase_domain_1/3'>alpha beta hydrolase fold</scene>.The C-terminal domain of lipoprotein lipase is composed of twelve beta strands which form a "<scene name='87/877513/Just_barrel_domain_1/1'>barrel domain</scene>". | ||
=== GPIHBP1 === | === GPIHBP1 === | ||
