Sandbox Reserved 1760: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The <scene name='93/934004/Binding_pocket/2'>binding pocket</scene> for PLP are semi-exposed to the "outside world" but also slightly hidden into the protein. Having binding pockets only slightly exposed can help prevent other competitive substrates from binding and and inhibiting the enzyme. | The <scene name='93/934004/Binding_pocket/2'>binding pocket</scene> for PLP are semi-exposed to the "outside world" but also slightly hidden into the protein. Having binding pockets only slightly exposed can help prevent other competitive substrates from binding and and inhibiting the enzyme. | ||
The substrate PLP has a phosphate group that is surrounded by other polar amino acids but the rest of the substrate, the carbons are surrounded by other non-polar amino acids to satisfy the needs of the <scene name='93/934004/Polar_non-polar_with_plp/1'>substrate and active site</scene>. PLP would not be very stable if the polar/hydrophilic portions of the substrate were trying to interact with all surrounding non-polar/hydrophobic amino acids. This allows interactions such as hydrogen bonding and pi-stacking to stabilize and bind a substrate in an active site. | |||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
