Sandbox Reserved 434
From Proteopedia
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Vanin-1 binds with 3 unique ligands including PEG (DI(HYDROXYETHYL)ETHER), NAG (N-ACETYL-D-GLUCOSAMINE) and RRV ((2R)-2,4-dihydroxy-N-[(3S)-3-hydroxy-4-phenylbutyl]-3,3-dimethylbutanamide). NAG and RRV both bind in the alpha helixes and beta strands but PEG only binds to the beta strands. | Vanin-1 binds with 3 unique ligands including PEG (DI(HYDROXYETHYL)ETHER), NAG (N-ACETYL-D-GLUCOSAMINE) and RRV ((2R)-2,4-dihydroxy-N-[(3S)-3-hydroxy-4-phenylbutyl]-3,3-dimethylbutanamide). NAG and RRV both bind in the alpha helixes and beta strands but PEG only binds to the beta strands. | ||
| + | Vanin 1 is a key protein that is involved in the breakdown of pantetheine to panthothenic acid and cysteamine. These proteins are associated with many metabolic diseases like type 2 diabetes. Understanding the binding interaction would give insight into treating these diseases more effectively. Vanin 1 has three catalytic residues (Glu79, Lys178 and Cys211) that represents the active site of the enzyme.The active site is located in the center of the enzyme in between the two sub-units. It was discovered that Glu79 and Lys178 were responsible for orienting and activating Cys211 to catalyze the reaction. | ||
<scene name='48/483891/Alpha_and_beta_structures/2'>Alpha and Beta Structures</scene> | <scene name='48/483891/Alpha_and_beta_structures/2'>Alpha and Beta Structures</scene> | ||
Revision as of 19:22, 10 April 2016
| This Sandbox is Reserved from January 19, 2016, through August 31, 2016 for use for Proteopedia Team Projects by the class Chemistry 423 Biochemistry for Chemists taught by Lynmarie K Thompson at University of Massachusetts Amherst, USA. This reservation includes Sandbox Reserved 425 through Sandbox Reserved 439. |
Pantetheinase (4CYG)[1]
by [Luke Schnitzler, Patrick Tonne, Owen O'Connor, Tyler Russell, Nicholas Sant]
Student Projects for UMass Chemistry 423 Spring 2016
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