Sandbox Reserved 1176
From Proteopedia
(Difference between revisions)
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== Structure == | == Structure == | ||
| - | Within the center of the protein is the ===Ligand Binding Pocket===. This pocket is comprised of several key amino acid resides. The first reside is a Phenylalanine at position F358. The purpose of this amino acid is to | + | Within the center of the protein is the ===Ligand Binding Pocket===. This pocket is comprised of several key amino acid resides. The first reside is a Phenylalanine at position F358. The purpose of this amino acid is to take part in a network of hydrophobic stacking interactions. These interactions stabilize the Y324 and W321 residues. These are crucial interactions because the Y324 is the amino acid residue that directly interacts for the L13 residue of the NTS ligand via Van der Waals interactions. Without the hydrophobic stacking interactions that are facilitated by the F358 this binding interaction would not occur. The W321 residue also partakes in these stacking interactions. The W321 serves as the boundary between the ligand binding pocket and the sodium binding pocket. |
<scene name='72/721547/Hydrophobic_binding_pocket/1'>Hydrophobic Binding Pocket</scene> | <scene name='72/721547/Hydrophobic_binding_pocket/1'>Hydrophobic Binding Pocket</scene> | ||
== Disease == | == Disease == | ||
Revision as of 17:19, 25 March 2016
| This Sandbox is Reserved from Jan 11 through August 12, 2016 for use in the course CH462 Central Metabolism taught by R. Jeremy Johnson at the Butler University, Indianapolis, USA. This reservation includes Sandbox Reserved 1160 through Sandbox Reserved 1184. |
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Rattus norevegicus NTSR1
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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
