Sandbox Reserved 1630

From Proteopedia

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{{Sandbox_Reserved_BHall_F20}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
{{Sandbox_Reserved_BHall_F20}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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==Your Heading Here (maybe something like 'Structure')==
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==Protein structure==
<StructureSection load='6Y9J' size='340' side='right' caption='Caption for this structure' scene=''>
<StructureSection load='6Y9J' size='340' side='right' caption='Caption for this structure' scene=''>
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
 
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
 
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== Function of your Protein ==
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== Function of your Protein == the protein Epa1ACBL2Epa9–Galb1-4Glc is from Candida glabrata, which is a human fungal pathogen. <scene name='86/861612/Ligands/1'> function of the protein is for sugar binding</scene>. The protein is a receptor. It interacts with calcium ions, chloride ions, and sodium ions.
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== Biological relevance and broader implications ==
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== Biological relevance and broader implications == The protein is associated with the fungus Candida Glabrata. It is a natural yeast fungus that, if it enters the bloodstream, can have life-threatening complications for people with suppressed or weakened immune systems. The protein is important to study because it can help to determine how diverse structural hot spots effect host cell binding and ligand binding specificity.
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== Important amino acids ==
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== Important amino acids == <scene name='86/861612/Ligands_blue/3'>ligand are calcium, chloride, and sodium ions</scene> the ligands play a vital role in the protein because they give signals that determine the specificity of how the protein binds.
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the protein lacks a cataytic triad as it is a lectin and lacks enzymatic activity
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== Structural highlights ==
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<scene name='86/861612/Protein_sturcture/1'>view of active site</scene>
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== Other important features ==
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== Structural highlights ==
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<scene name='86/861612/Secondary_structure/1'>secondary structure of the protein</scene> alpha helix in red, beta strand in yellow, turn in purple, coil/loop in white
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
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<scene name='86/861612/Spacefill/1'>spacefill scene</scene> the spacefill view of the protein allows for a view of the intermolecular forces in the protein and to be able to see the size of the protein. Can also see where the ligands bind to the receptor areas in the protein
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The macromolecule content of the protein shows that it has a total structure weight of 29.92 kDa, the residue count is 232, and it has one unique protein chain., The A chains of the protein has a sequence length of 262. The protein has 4 helices. There are 14 parts to the beta strand. the ligands each bind to the protein through ionic bonding.
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== Other important features ==
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the protein contains structural motifs that it has in common with other proteins of the epa family. it also shares motif loops such as CBL2, and DcisD. these are both structural loops of the protein. CBL2 is important for determining ligand binding specificity. many of the motifs are used to maintain protein structure.
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The protein interacts with other proteins of its protein family. these interactions are important because they allow for larger protein interactions.
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The dimerization interface of the protein which allows for it to make larger structure is important because it allows for the protein to stabilize its structure.
</StructureSection>
</StructureSection>
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== References ==
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== References ==
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<references/>
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<ref>PMID:32669365</ref>
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Functional reprogramming of Candida glabrata epithelial adhesins: the role of conserved and variable structural motifs in ligand binding

Current revision

This Sandbox is Reserved from 09/18/2020 through 03/20/2021 for use in CHEM 351 Biochemistry taught by Bonnie Hall at Grand View University, Des Moines, IA. This reservation includes Sandbox Reserved 1628 through Sandbox Reserved 1642.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Protein structure

Caption for this structure

Drag the structure with the mouse to rotate

References

[1] Functional reprogramming of Candida glabrata epithelial adhesins: the role of conserved and variable structural motifs in ligand binding

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