Sandbox Reserved 470: Difference between revisions

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OCA, Sophia Lemieux

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 ==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==
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-GAPDH has two domains, a GAPDH-like, C-terminal domain, and an NAD Binding Domain.
+*While GAPDH possesses four cysteine residues, its <scene name='Sandbox_Reserved_470/Active_site_gapdh/1'>active site</scene> is located around <scene name='Sandbox_Reserved_470/Cysteine_active_site/1'>Cysteine 149</scene>, which is responsible for inhibition of glycolysis and fermentation by iodoacetic acid. '''<ref>''' Boyer, Paul D.. "The Enzymes - Paul D. Boyer - Google Books." Google Books. N.p., n.d. Web. 1 May 2012. '''[<http://books.google.com/books?id=r6SRFsxYFYwC&pg=PA20&lpg=PA20&dq=GAPDH+cysteine+149&source=bl&ots=0CWwdduzGB&sig=Lb8PtWq7EGdwyvdAnFI_rHYG3tU&hl=en&sa=X&ei=2PyhT-WtHJSy8QTjtsnTCA&ved=0CDMQ6AEwAg#v=onepage&q=GAPDH%20cysteine%20149&f=false>]'''. '''</ref>'''
-*The NAD (Nucleotide) Binding Domain is an Alpha Beta 3-Layer(α-β-α) Sandwich, including  amino acids 1-138 and 301-340 on chains O and Q .   Its [http://en.wikipedia.org/wiki/CATH CATH] reports a Rossmann fold and a classification as an [http://en.wikipedia.org/wiki/Oxidoreductase oxidoreductase].
+*GAPDH has two domains, a GAPDH-like, C-terminal domain, and an NAD Binding Domain.
+:The <scene name='Sandbox_Reserved_470/Nad_binding_domain/3'>NAD (Nucleotide) Binding Domain </scene> is an Alpha Beta 3-Layer(α-β-α) Sandwich, including  amino acids 1-138 and 301-340 on chains O and Q .   Its [http://en.wikipedia.org/wiki/CATH CATH] reports a Rossmann fold and a classification as an [http://en.wikipedia.org/wiki/Oxidoreductase oxidoreductase].
-*The 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.  '''<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:GAPDH homotetramer 2.png|300 px]]
 ==Importance==
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 ==References==
 <references/>
+#↑Boyer, Paul D.. "The Enzymes - Paul D. Boyer - Google Books." Google Books. N.p., n.d. Web. 1 May 2012. '''<ref>''' Boyer, Paul D.. "The Enzymes - Paul D. Boyer - Google Books." Google Books. N.p., n.d. Web. 1 May 2012. '''[<http://books.google.com/books?id=r6SRFsxYFYwC&pg=PA20&lpg=PA20&dq=GAPDH+cysteine+149&source=bl&ots=0CWwdduzGB&sig=Lb8PtWq7EGdwyvdAnFI_rHYG3tU&hl=en&sa=X&ei=2PyhT-WtHJSy8QTjtsnTCA&ved=0CDMQ6AEwAg#v=onepage&q=GAPDH%20cysteine%20149&f=false>]'''. '''</ref>'''
 #↑"GAPDH glyceraldehyde-3-phosphate dehydrogenase [Homo sapiens] - Gene - NCBI." National Center for Biotechnology Information. N.p., n.d. Web. 1 May 2012.  '''<ref>'''"GAPDH glyceraldehyde-3-phosphate dehydrogenase [Homo sapiens] - Gene - NCBI." National Center for Biotechnology Information. N.p., n.d. Web. 1 May 2012. '''[<http://www.ncbi.nlm.nih.gov/gene/2597>]'''. '''<ref/>'''
 #↑"Glyceraldehyde 3-phosphate dehydrogenase." Stanford University. N.p., n.d. Web. 22 Apr. 2012. '''<ref>'''"Glyceraldehyde 3-phosphate dehydrogenase." Stanford University. N.p., n.d. Web. 22 Apr. 2012. '''[<http://www.stanford.edu/~mmogri/bio/gapdh/structure.html>]'''. '''</ref>'''