Sandbox Reserved 1694: Difference between revisions
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In the structure INPP1D54A, there is a mutation in the amino acid aspartic acid (D)54 and causes it to change to alanine (A)54 (<scene name='89/892737/Alanine/1'>mutation in D54</scene>). This mutation does not impact the substrate affinity but does decrease the activity of INPP1. <ref name="dollins" /> | In the structure INPP1D54A, there is a mutation in the amino acid aspartic acid (D)54 and causes it to change to alanine (A)54 (<scene name='89/892737/Alanine/1'>mutation in D54</scene>). This mutation does not impact the substrate affinity but does decrease the activity of INPP1. <ref name="dollins" /> | ||
[[Image:Motif_Copy.png | thumb]] | [[Image:Motif_Copy.png | thumb]] | ||
A six amino acid <scene name='89/892737/Motif/1'>motif</scene>, DPIDxT anchors the metal-binding sites in the protein that are likely involved in catalysis while the metal binds to the substrate. <ref name="dollins" /> The sixth amino acid, x, is not as important as the other five, however, it can be any amino acid depending on the related crystallized structure to INPP1D54A or to a similar protein. Also, lithium is an uncompetitive inhibitor for this | A six amino acid <scene name='89/892737/Motif/1'>motif</scene>, DPIDxT anchors the metal-binding sites in the protein that are likely involved in catalysis while the metal binds to the substrate. <ref name="dollins" /> The sixth amino acid, x, is not as important as the other five, however, it can be any amino acid depending on the related crystallized structure to INPP1D54A or to a similar protein. Also, lithium is an uncompetitive inhibitor for this enzyme and when it binds to a metal site (metal site 3 in the lower image B) it causes the protein not to function properly. | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references /> | <references /> | ||
