Sandbox Reserved 470: Difference between revisions
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==Introduction== | ==Introduction== | ||
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*'''[[Glyceraldehyde-3-phosphate Dehydrogenase]]''' | *'''[[Glyceraldehyde-3-phosphate Dehydrogenase]]''' ([http://www.rcsb.org/pdb/home/home.do RSCB] (PDB)used:3dpg) | ||
<Structure load='3gpd' size='350' frame='true' align='right' caption='Glyceraldehyde-3-phosphate Dehydrogenase' scene='Insert optional scene name here' />(abbreviated as GAPDH or the less common G3PDH) (EC 1.2.1.12) ~37kDa is a well-known [http://en.wikipedia.org/wiki/Enzyme enzyme] which catalyzes the sixth step of [[glycolysis]], a reversible cytosolic process in [http://en.wikipedia.org/wiki/Eukaryote eukaryotes] which involves the breakdown of glucose for energy and carbon molecules. Along with its role in glycolysis and [http://en.wikipedia.org/wiki/Gluconeogenesis gluconeogenesis], recent research has determined that GAPDH is actually a multifunctional protein, as it has numerous defined, non-metabolic functions involved in multiple subcellular processes including [http://en.wikipedia.org/wiki/Transcription transcription] activation, ER to Golgi transportation, transcriptional control of histone [http://en.wikipedia.org/wiki/Gene_Expression gene expression], nuclear membrane fusion, neuronal initiation of [http://en.wikipedia.org/wiki/Apoptosis apoptosis], microtubule bundling, phosphotransferase activity, prostate cancer progression, recognizing fraudulently incorporated nucleotides in DNA, and maintaining [http://en.wikipedia.org/wiki/Telomere telomere] structures. Research also shows that it possibly has a direct involvement in cellular phenotype of human [http://en.wikipedia.org/wiki/Neurodegeneration neurodegenerative] disorders, especially those characterized by expansion of [http://en.wikipedia.org/wiki/CAG_Triplet_Repeat_Disorders CAG repeats]. | <Structure load='3gpd' size='350' frame='true' align='right' caption='Glyceraldehyde-3-phosphate Dehydrogenase' scene='Insert optional scene name here' />(abbreviated as GAPDH or the less common G3PDH) (EC 1.2.1.12) ~37kDa is a well-known [http://en.wikipedia.org/wiki/Enzyme enzyme] which catalyzes the sixth step of [[glycolysis]], a reversible cytosolic process in [http://en.wikipedia.org/wiki/Eukaryote eukaryotes] which involves the breakdown of glucose for energy and carbon molecules. Along with its role in glycolysis and [http://en.wikipedia.org/wiki/Gluconeogenesis gluconeogenesis], recent research has determined that GAPDH is actually a multifunctional protein, as it has numerous defined, non-metabolic functions involved in multiple subcellular processes including [http://en.wikipedia.org/wiki/Transcription transcription] activation, ER to Golgi transportation, transcriptional control of histone [http://en.wikipedia.org/wiki/Gene_Expression gene expression], nuclear membrane fusion, neuronal initiation of [http://en.wikipedia.org/wiki/Apoptosis apoptosis], microtubule bundling, phosphotransferase activity, prostate cancer progression, recognizing fraudulently incorporated nucleotides in DNA, and maintaining [http://en.wikipedia.org/wiki/Telomere telomere] structures. Research also shows that it possibly has a direct involvement in cellular phenotype of human [http://en.wikipedia.org/wiki/Neurodegeneration neurodegenerative] disorders, especially those characterized by expansion of [http://en.wikipedia.org/wiki/CAG_Triplet_Repeat_Disorders CAG repeats]. | ||
==Structure== | ==Structure== | ||
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:The <scene name='Sandbox_Reserved_470/Gapdh-like_c-terminal_domain/3'>GAPDH-like, C-terminal domain</scene>GAPDH-like, C-terminal domain (Catalytic domain) is an Alpha Beta 2-Layer(α-β) Sandwich, including amino acids 139 - 300 on chains O and Q . Its CATH reports a holo-D-Glyceraldehyde-3-Phosphate Dehydrogenase, (domain 2) and a classification as an oxidoreductase (aldehyde(D)-NAD(A)). | :The <scene name='Sandbox_Reserved_470/Gapdh-like_c-terminal_domain/3'>GAPDH-like, C-terminal domain</scene>GAPDH-like, C-terminal domain (Catalytic domain) is an Alpha Beta 2-Layer(α-β) Sandwich, including amino acids 139 - 300 on chains O and Q . Its CATH reports a holo-D-Glyceraldehyde-3-Phosphate Dehydrogenase, (domain 2) and a classification as an oxidoreductase (aldehyde(D)-NAD(A)). | ||
*Depending on the environment, including variations in temperature and acidity, GAPDH can have different structural qualities and physical properties. In some cases, it is observed as a twinned structure with an α/β barrel. | *Depending on the environment, including variations in temperature and acidity, GAPDH can have different structural qualities and physical properties. In some cases, it is observed as a twinned structure with an α/β barrel. '''<ref>'''Watson, H.C., and J.C. Campbell. "Twinning In Crystals Of Human Skeletal Muscle D-Glyceraldehyde-3-Phosphate Dehydrogenase." RCSB Protein Data Bank. N.p., 27 Oct. 1983. Web. 28 Apr. 2012. '''[<www.rcsb.org/pdb/explore/explore.do?structureId=3gpd>]'''. '''</ref>''' | ||
[[Image: | [[Image:GAPDH homotetramer 2.png|300 px]] | ||
==Importance== | ==Importance== | ||
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