Sandbox Reserved 1458
From Proteopedia
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Here is a <scene name='79/799586/4x2z1/2'>cartoon view</scene> of PLpro, it's main secondary features are mainly beta sheets and with alpha helixes and a little less random coils. | Here is a <scene name='79/799586/4x2z1/2'>cartoon view</scene> of PLpro, it's main secondary features are mainly beta sheets and with alpha helixes and a little less random coils. | ||
In this <scene name='79/799586/4x2zb/1'>cartoon view</scene> the most important tertiary and quaternary structures of PLpro are highlighted. They include the P4 residues which is the resides that the most impact on catalytic efficiency. | In this <scene name='79/799586/4x2zb/1'>cartoon view</scene> the most important tertiary and quaternary structures of PLpro are highlighted. They include the P4 residues which is the resides that the most impact on catalytic efficiency. | ||
- | This is a <scene name='79/799586/4z2zspacefill/1'>space filling</scene> view of PLpro where it shows how much space the atoms take up in the protein. | + | This is a <scene name='79/799586/4z2zspacefill/1'>space filling</scene> view of PLpro where it shows how much space the atoms take up in the protein. This model is useful because it allows us to see shape and relative dimension of the molecule as well as the shape of the surface. |
Here is a <scene name='79/799586/4x2zhydrophobicity/1'>hydrophobicity-focused view</scene> of PLpro, the importance of hydrophobic and hydrophilic regions are that they determine how the proteins fold and that is the case in PLpro as well. PLpro has a mix of hydrophobic and hydrophilic regions. | Here is a <scene name='79/799586/4x2zhydrophobicity/1'>hydrophobicity-focused view</scene> of PLpro, the importance of hydrophobic and hydrophilic regions are that they determine how the proteins fold and that is the case in PLpro as well. PLpro has a mix of hydrophobic and hydrophilic regions. | ||
Here is a view of the <scene name='79/799586/4x2zligand/1'>ligand</scene>. The important chemical features of the ligand is that they form H bonds with each other and have metal interactions with Zinc. The amino acids that interact with the ligand are Cystine, Threonine and Arginine. Cystine interacts with Zn through metal interactions as well as forms H bonds with other Cystines and Threonine. | Here is a view of the <scene name='79/799586/4x2zligand/1'>ligand</scene>. The important chemical features of the ligand is that they form H bonds with each other and have metal interactions with Zinc. The amino acids that interact with the ligand are Cystine, Threonine and Arginine. Cystine interacts with Zn through metal interactions as well as forms H bonds with other Cystines and Threonine. |
Revision as of 04:15, 3 December 2018
This Sandbox is Reserved from October 22, 2018 through April 30, 2019 for use in the course Biochemistry taught by Bonnie Hall at the Grand View University, Des Moines, IA USA. This reservation includes Sandbox Reserved 1456 through Sandbox Reserved 1470. |
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Structure of PLpro
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References
- ↑ Kong L, Shaw N, Yan L, Lou Z, Rao Z. Structural View and Substrate Specificity of Papain-like Protease from Avian Infectious Bronchitis Virus. J Biol Chem. 2015 Mar 13;290(11):7160-8. doi: 10.1074/jbc.M114.628636. Epub 2015 , Jan 21. PMID:25609249 doi:http://dx.doi.org/10.1074/jbc.M114.628636