Sandbox ggc6
From Proteopedia
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== Function == | == Function == | ||
| - | One of nine known FABP, members of the superfamily of lipid-binding proteins, that are believed to be involved in fatty acid uptake, transport, and metabolism. The brain is made up of approximately 60% fat; unsaturated fatty acids play an important role in brain integrity and performance. Essential fatty acids aid in the synthesis and functions of neurotransmitters, and help the immune system by signaling the brain. | + | One of nine known FABP, members of the superfamily of lipid-binding proteins, that are believed to be involved in fatty acid uptake, transport, and metabolism. The brain is made up of approximately 60% fat; unsaturated fatty acids play an important role in brain integrity and performance. Essential fatty acids aid in the synthesis and functions of neurotransmitters, and help the immune system by signaling the brain. |
== Structure == | == Structure == | ||
| - | The FABP genes each have 4 exons and 3 introns with many residing in the same chromosomal region. Between the different know FABP the amino acid sequence varies widely but the three dimensional sequence is heavily conserved. <scene name='75/752265/Secondary_structures/1'>Secondary structures</scene>: It consist of ten antiparallel β strands and two short α helices. The ten antiparallel β strands are arranged into two nearly orthogonal 5-stranded β sheets that surround the interior binding cavity. B-FABP is commonly bound to poly-unsaturated fatty acids; this gives the ligand in the binding region a <scene name='75/752265/Ligand_ball_and_stick/1'>U-Shaped</scene> confirmation. | + | The FABP genes each have 4 exons and 3 introns with many residing in the same chromosomal region. Between the different know FABP the amino acid sequence varies widely but the three dimensional sequence is heavily conserved. <scene name='75/752265/Secondary_structures/1'>Secondary structures</scene>: It consist of ten antiparallel β strands and two short α helices. The ten antiparallel β strands are arranged into two nearly orthogonal 5-stranded β sheets that surround the interior binding cavity. B-FABP is commonly bound to poly-unsaturated fatty acids; this gives the ligand in the binding region a <scene name='75/752265/Ligand_ball_and_stick/1'>U-Shaped</scene> confirmation. In B-FABP the hydrophobic regions are <scene name='75/752265/Polarnonpolar/1'>orientated</scene> towards the central where they form Van Der Waals interactions with the ligand leaving the polar molecules to protect from oxygen radicals. |
== Disease == | == Disease == | ||
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Oleic acid, the unsaturated fatty acid bound, is one of six unsaturated fatty acids that have been linked to Alzheimer's Disease. Oxidant-stress and peroxidation of these UFA's create oxygenated metabolites that damage the central nervous system. Besides Alzheimer's disease the oxygenated damage help the pathogenesis of many neurodegenerative disorders; they are used to measure the oxidative stress on the brain. | Oleic acid, the unsaturated fatty acid bound, is one of six unsaturated fatty acids that have been linked to Alzheimer's Disease. Oxidant-stress and peroxidation of these UFA's create oxygenated metabolites that damage the central nervous system. Besides Alzheimer's disease the oxygenated damage help the pathogenesis of many neurodegenerative disorders; they are used to measure the oxidative stress on the brain. | ||
| - | Color Key: | ||
| - | Cyan-Alpha Helix; | ||
| - | Magenta-Beta Sheet; | ||
| - | Yellow-Arg 514; | ||
| - | Lime Green-All Glutamate; | ||
| - | Dark Blue-Backbone/Main Chain; | ||
| - | Maroon-All Lys; | ||
| - | Black-Ser509; | ||
| - | Orange-Cys502. The N-free pyrazole of 22 interacts with Glu500 and Cys502 in the hinge region by two hydrogen bonds <ref>PMID: 23414845</ref>. . | ||
| - | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 02:42, 23 April 2018
CRYSTAL STRUCTURE OF HUMAN BRAIN FATTY ACID BINDING PROTEIN OLEIC ACID
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You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Contents |
Function
One of nine known FABP, members of the superfamily of lipid-binding proteins, that are believed to be involved in fatty acid uptake, transport, and metabolism. The brain is made up of approximately 60% fat; unsaturated fatty acids play an important role in brain integrity and performance. Essential fatty acids aid in the synthesis and functions of neurotransmitters, and help the immune system by signaling the brain.
Structure
The FABP genes each have 4 exons and 3 introns with many residing in the same chromosomal region. Between the different know FABP the amino acid sequence varies widely but the three dimensional sequence is heavily conserved. : It consist of ten antiparallel β strands and two short α helices. The ten antiparallel β strands are arranged into two nearly orthogonal 5-stranded β sheets that surround the interior binding cavity. B-FABP is commonly bound to poly-unsaturated fatty acids; this gives the ligand in the binding region a confirmation. In B-FABP the hydrophobic regions are towards the central where they form Van Der Waals interactions with the ligand leaving the polar molecules to protect from oxygen radicals.
Disease
Oleic acid, the unsaturated fatty acid bound, is one of six unsaturated fatty acids that have been linked to Alzheimer's Disease. Oxidant-stress and peroxidation of these UFA's create oxygenated metabolites that damage the central nervous system. Besides Alzheimer's disease the oxygenated damage help the pathogenesis of many neurodegenerative disorders; they are used to measure the oxidative stress on the brain.
References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
