Sandbox Reserved 1632: Difference between revisions

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== Biological relevance and broader implications ==

Candida glabrata is a fungus of high concern as it infects the host through the bloodstream. Unfortunately, this is a life-threatening infection for humans and upwards of 29% of all cases are life-threatening. As this does affect the human race is it of high relevance to study in health sciences. Understanding how this fungus can infect the bloodstream is needed to slow and possibly stop Candida glabrata from infecting other people. The approach in this paper is on the epithelial adhesions and altering their composition around the binding site. By altering conversed and un-conserved areas in its binding site we can better understand what hot spots are needed for good binding to the carbohydrates on the human epithelial cells.

Candida glabrata is a fungus of high concern as it infects the host through the bloodstream. Unfortunately, this is a life-threatening infection for humans and upwards of 29% of all cases are life-threatening. As this does affect the human race is it of high relevance to study in health sciences. Understanding how this fungus can infect the bloodstream is needed to slow and possibly stop Candida glabrata from infecting other people. The approach in this paper is on the epithelial adhesions and altering their composition around the binding site. By altering conversed and un-conserved areas in its binding site we can better understand what hot spots are needed for good binding to the carbohydrates on the human epithelial cells. In this page we will highlight Epa9 specifically and how it is able to bind compared to other mutants created from the paper.

== Important amino acids ==

The type of protein that we are looking at is an adhesion protein, so it does not function as an enzyme. It does not have a catalytic triad within the active site. Though there are some important amino acid residues to highlight as they interact with the ligand (lactose). In the diagram of the protein, we can look to see the all-red ball stick structures by the ligand are the amino acid residues interacting with the ligand. <scene name='86/861614/Protein_view_2/5'>These would be Arg258, Asp257, Asp196, and Asp197.</scene>. They are all interacting via hydrogen bonds as depicted with this image. [[Image:Inked4CP0 view of hydrogen bond interactions on ligand LI.jpg | thumb]]

The type of protein that we are looking at is an adhesion protein, so it does not function as an enzyme. It does not have a catalytic triad within the active site. Though there are some important amino acid residues to highlight as they interact with the ligand (lactose). In the diagram of the protein, we can look to see the all-red ball stick structures by the ligand are the amino acid residues interacting with the ligand. <scene name='86/861614/Protein_view_2/5'>These would be Arg258, Asp257, Asp196, and Asp197.</scene>. They are all interacting via hydrogen bonds as depicted with this image off to the right. In the image, the hydrogen bonds involved are circled and we can see that there are only six hydrogen bonds that are binding the lactose to Epa9, which could account for a low binding affinity towards smaller carbohydrates. [[Image:Inked4CP0 view of hydrogen bond interactions on ligand LI.jpg | thumb]]

== Structural highlights ==

Sandbox Reserved 1632: Difference between revisions

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 == Biological relevance and broader implications ==
-Candida glabrata is a fungus of high concern as it infects the host through the bloodstream. Unfortunately, this is a life-threatening infection for humans and upwards of 29% of all cases are life-threatening. As this does affect the human race is it of high relevance to study in health sciences. Understanding how this fungus can infect the bloodstream is needed to slow and possibly stop Candida glabrata from infecting other people. The approach in this paper is on the epithelial adhesions and altering their composition around the binding site. By altering conversed and un-conserved areas in its binding site we can better understand what hot spots are needed for good binding to the carbohydrates on the human epithelial cells.
+Candida glabrata is a fungus of high concern as it infects the host through the bloodstream. Unfortunately, this is a life-threatening infection for humans and upwards of 29% of all cases are life-threatening. As this does affect the human race is it of high relevance to study in health sciences. Understanding how this fungus can infect the bloodstream is needed to slow and possibly stop Candida glabrata from infecting other people. The approach in this paper is on the epithelial adhesions and altering their composition around the binding site. By altering conversed and un-conserved areas in its binding site we can better understand what hot spots are needed for good binding to the carbohydrates on the human epithelial cells. In this page we will highlight Epa9 specifically and how it is able to bind compared to other mutants created from the paper.
 == Important amino acids ==
-The type of protein that we are looking at is an adhesion protein, so it does not function as an enzyme. It does not have a catalytic triad within the active site. Though there are some important amino acid residues to highlight as they interact with the ligand (lactose). In the diagram of the protein, we can look to see the all-red ball stick structures by the ligand are the amino acid residues interacting with the ligand. <scene name='86/861614/Protein_view_2/5'>These would be Arg258, Asp257, Asp196, and Asp197.</scene>. They are all interacting via hydrogen bonds as depicted with this image. [[Image:Inked4CP0 view of hydrogen bond interactions on ligand LI.jpg | thumb]]
+The type of protein that we are looking at is an adhesion protein, so it does not function as an enzyme. It does not have a catalytic triad within the active site. Though there are some important amino acid residues to highlight as they interact with the ligand (lactose). In the diagram of the protein, we can look to see the all-red ball stick structures by the ligand are the amino acid residues interacting with the ligand. <scene name='86/861614/Protein_view_2/5'>These would be Arg258, Asp257, Asp196, and Asp197.</scene>. They are all interacting via hydrogen bonds as depicted with this image off to the right. In the image, the hydrogen bonds involved are circled and we can see that there are only six hydrogen bonds that are binding the lactose to Epa9, which could account for a low binding affinity towards smaller carbohydrates. [[Image:Inked4CP0 view of hydrogen bond interactions on ligand LI.jpg | thumb]]
 == Structural highlights ==