Sandbox Reserved 427: Difference between revisions

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-Vitamin D binding protein is very similar to <scene name='48/483884/Hsa/1'>HSA</scene> based on sequence similarity as well as an almost identical tertiary structure. However, HSA binds to actin instead, and is actually unable to bind to Vitamin D3. Based on what you have learned about the binding nature in domain I of Vitamin D Binding Protein, hypothesize a reason why HSA is unable to bind to Vitamin D3, but Vitamin D binding protein can. The following scenes should help guide your thinking = Domain I Helices 2,3,4 HSA; Domain I Helices 2,3,4 Vitamin D binding Protein.
+Vitamin D binding protein is very similar to <scene name='48/483884/Cartoonhsa/1'>Human Serum Albumin(HSA)</scene>based on sequence similarity as well as a similar <scene name='48/483884/Cartoondpb/1'>tertiary structure</scene>. However, the two proteins bind very different ligands. HSA binds to actin instead, and is actually unable to bind to Vitamin D3. Based on what you have learned about the binding nature in domain I, and looking at the structures of the two proteins, hypothesize a reason why the two proteins bind different ligands. How can altering only a couple of amino acids so greatly alter the final tertiary structure of proteins?
 ==See Also==
 *[[1kxp]]

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