Sandbox Reserved 1632: Difference between revisions

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== Other important features ==

To look further into the structure studied we are going to compare two of the versions of the Epa's from the paper cited below. First looking at Epa9, this structure off to the right we can see the elongated loop 1. It was highlighted that this loop is important to the structure as it binds bigger sugars than an Epa1. It stays in an open state when bound to a bigger sugar, but as shown here it is in a more closed state as it is bound to a smaller sugar. Now looking at another structure for comparison, a mixed version of Epa9, but the only difference is that its CBL2 loop is from Epa1.

To look further into the structure studied we are going to compare two of the versions of the Epa's from the paper cited below. First looking at <scene name='86/861614/Cbls_and_outer_loops/5'>Epa9</scene>, this structure off to the right we can see the elongated loop 1. It was highlighted that this loop is important to the structure as it binds bigger sugars than an Epa1. It stays in an open state when bound to a bigger sugar, but as shown here it is in a more closed state as it is bound to a smaller sugar. Now looking at another structure for comparison, a mixed version of Epa9, but the only difference is that its CBL2 loop is from Epa1. The reason for comparing these two is to show that the change in the CBL2 being changed how by little interaction changes in the angles in the binding, that it can change the binding specificity of the protein to different carbohydrates. The exchange of the CBL2 does not entirely change the binding specificity of the protein but makes a novel binding pattern. Comparing these two there is not much difference to the eye, but the angle and distance that carbon 6 in the glucose ring from the key residues has a big impact. In the mixed Epa9, this distance change is actually why the binding pattern changes. It is to accommodate the change and find a better binding carbohydrate.

</StructureSection>

Sandbox Reserved 1632: Difference between revisions

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@@ Line 17: / Line 17: @@
 == Other important features ==
-To look further into the structure studied we are going to compare two of the versions of the Epa's from the paper cited below. First looking at Epa9, this structure off to the right we can see the elongated loop 1. It was highlighted that this loop is important to the structure as it binds bigger sugars than an Epa1. It stays in an open state when bound to a bigger sugar, but as shown here it is in a more closed state as it is bound to a smaller sugar. Now looking at another structure for comparison, a mixed version of Epa9, but the only difference is that its CBL2 loop is from Epa1.
+To look further into the structure studied we are going to compare two of the versions of the Epa's from the paper cited below. First looking at <scene name='86/861614/Cbls_and_outer_loops/5'>Epa9</scene>, this structure off to the right we can see the elongated loop 1. It was highlighted that this loop is important to the structure as it binds bigger sugars than an Epa1. It stays in an open state when bound to a bigger sugar, but as shown here it is in a more closed state as it is bound to a smaller sugar. Now looking at another structure for comparison, a mixed version of Epa9, but the only difference is that its CBL2 loop is from Epa1. The reason for comparing these two is to show that the change in the CBL2 being changed how by little interaction changes in the angles in the binding, that it can change the binding specificity of the protein to different carbohydrates. The exchange of the CBL2 does not entirely change the binding specificity of the protein but makes a novel binding pattern. Comparing these two there is not much difference to the eye, but the angle and distance that carbon 6 in the glucose ring from the key residues has a big impact. In the mixed Epa9, this distance change is actually why the binding pattern changes. It is to accommodate the change and find a better binding carbohydrate.
 </StructureSection>