Sandbox Reserved 1550
From Proteopedia
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<Structure load='1tou' size='350' frame='true' align='right' caption='Fatty Acid Binding Protein' scene='Insert optional scene name here' />{{ Sandbox_Reserved_GGC_BHCM4100_1}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | <Structure load='1tou' size='350' frame='true' align='right' caption='Fatty Acid Binding Protein' scene='Insert optional scene name here' />{{ Sandbox_Reserved_GGC_BHCM4100_1}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
== '''Fatty Acid Binding Protein''' == | == '''Fatty Acid Binding Protein''' == | ||
| + | Intracellular lipid chaperones known as fatty acid-binding proteins (FABPs) are a group of molecules that coordinate lipid responses in cells and are also strongly linked to metabolic and inflammatory pathways. FABPs are abundantly expressed 14–15 kDa proteins that reversibly bind hydrophobic ligands, such as saturated and unsaturated long-chain fatty acids, eicosanoids and other lipids, with high affinity. | ||
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
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== '''Function''' == | == '''Function''' == | ||
| + | Fatty Acids Binding Proteins maintain intracellular lipid homeostasis and also affect systemic lipid metabolism. They have very unique features that allow them to transport and metabolize long chain fatty acids. Studies have suggested that subtle three dimensional changes that occur upon ligand binding may promote specific FABP-protein or FABP-membrane interactions that ultimately determine the particular function of the FABP. | ||
| + | |||
| + | FABPs play a role in the transport of lipids to specific compartments in the cell: | ||
| + | |||
| + | - to lipid droplets for storage; | ||
| + | |||
| + | - to the endoplasmic reticulum for signalling, trafficking and membrane synthesis; | ||
| + | |||
| + | - to the mitochondria or peroxisome for oxidation; | ||
| + | |||
| + | - to cytosolic or other enzymes to regulate their activity; | ||
| + | |||
| + | - to the nucleus for the control of lipid-mediated transcriptional programs via nuclear hormone receptors (NHRs) or other transcription factors that respond to lipids; | ||
| + | |||
| + | - or even outside the cell to signal in an autocrine or paracrine manner. | ||
== '''Disease''' == | == '''Disease''' == | ||
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== '''Reference''' == | == '''Reference''' == | ||
Ringom, Rune; Axen, Eva; Uppenberg, Jonas; Lundbäck, Thomas; Rondahl, Lena; Barf, Tjeerd. (2004), Substituted benzylamino-6-(trifluoromethyl)pyrimidin-4(1H)-ones: a novel class of selective human A-FABP inhibitors. Elsevier BV., 14:4449-4452. https://doi.org/10.1016/j.bmcl.2004.06.058 | Ringom, Rune; Axen, Eva; Uppenberg, Jonas; Lundbäck, Thomas; Rondahl, Lena; Barf, Tjeerd. (2004), Substituted benzylamino-6-(trifluoromethyl)pyrimidin-4(1H)-ones: a novel class of selective human A-FABP inhibitors. Elsevier BV., 14:4449-4452. https://doi.org/10.1016/j.bmcl.2004.06.058 | ||
| + | |||
| + | Storch, Judith, and Lindsay McDermott. “Structural and functional analysis of fatty acid-binding proteins.” Journal of lipid research vol. 50 Suppl,Suppl (2009): S126-31. doi:10.1194/jlr.R800084-JLR200 | ||
Revision as of 20:53, 27 April 2019
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| This Sandbox is Reserved from May 28 through July 01, 2019 for use in the course Advanced Biochemistry BCHM 4100 taught by Tom Gluick at the Georgia Gwinnett College. This reservation includes Sandbox Reserved 1544 through Sandbox Reserved 1555. |
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Contents |
Fatty Acid Binding Protein
Intracellular lipid chaperones known as fatty acid-binding proteins (FABPs) are a group of molecules that coordinate lipid responses in cells and are also strongly linked to metabolic and inflammatory pathways. FABPs are abundantly expressed 14–15 kDa proteins that reversibly bind hydrophobic ligands, such as saturated and unsaturated long-chain fatty acids, eicosanoids and other lipids, with high affinity.
This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs.
Function
Fatty Acids Binding Proteins maintain intracellular lipid homeostasis and also affect systemic lipid metabolism. They have very unique features that allow them to transport and metabolize long chain fatty acids. Studies have suggested that subtle three dimensional changes that occur upon ligand binding may promote specific FABP-protein or FABP-membrane interactions that ultimately determine the particular function of the FABP.
FABPs play a role in the transport of lipids to specific compartments in the cell:
- to lipid droplets for storage;
- to the endoplasmic reticulum for signalling, trafficking and membrane synthesis;
- to the mitochondria or peroxisome for oxidation;
- to cytosolic or other enzymes to regulate their activity;
- to the nucleus for the control of lipid-mediated transcriptional programs via nuclear hormone receptors (NHRs) or other transcription factors that respond to lipids;
- or even outside the cell to signal in an autocrine or paracrine manner.
Disease
Relevance
Structural highlights
|
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
Reference
Ringom, Rune; Axen, Eva; Uppenberg, Jonas; Lundbäck, Thomas; Rondahl, Lena; Barf, Tjeerd. (2004), Substituted benzylamino-6-(trifluoromethyl)pyrimidin-4(1H)-ones: a novel class of selective human A-FABP inhibitors. Elsevier BV., 14:4449-4452. https://doi.org/10.1016/j.bmcl.2004.06.058
Storch, Judith, and Lindsay McDermott. “Structural and functional analysis of fatty acid-binding proteins.” Journal of lipid research vol. 50 Suppl,Suppl (2009): S126-31. doi:10.1194/jlr.R800084-JLR200
