Sandbox Reserved 1634

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== Biological relevance and broader implications ==
== Biological relevance and broader implications ==
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Epithelial Adhesins are important for fungi because they help the organism bind to the host so they can live, gain nurtrients and maintain its steady state. Candida Glabrata which house these epithelial adhesins are the 2nd major cause of clinical candidias, It is most prevelant in vaginal infections but can even cause systemic infections by entrance of the fungal cells in the bloodstream (Candidemia), especially prevalent in immunocompromised patients. it is important to study protiens like epithelial adhesins so we can better understand how fungi and other organisms infect the body, ny undertanding the role of these protiens we can begin to work on combat methods and long term immunity.
+
Epithelial Adhesins are important for fungi because they help the organism bind to the host so they can live, gain nutrients and maintain its steady state. Candida Glabrata which house these epithelial adhesins are the 2nd major cause of clinical candidiasis, It is most prevalent in vaginal infections but can even cause systemic infections by entrance of the fungal cells in the bloodstream (Candidemia), especially prevalent in immunocompromised patients. it is important to study proteins like epithelial adhesins so we can better understand how fungi and other organisms infect the body, by understanding the role of these proteins we can begin to work on combat methods and long term immunity.
== Important amino acids ==
== Important amino acids ==
i: DcisD = DD or asp 196,197 hydrogen bond with Gal b, metal interactions
i: DcisD = DD or asp 196,197 hydrogen bond with Gal b, metal interactions
with Ca+ that also has metal interactions with Gal b
with Ca+ that also has metal interactions with Gal b
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ii: Asn 241 is asparagine has metal interactions with ca+ and Gal b
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ii: Asn 256 is asparagine has metal interactions with ca+ and Gal b
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iii: Asp 243 metal interaction with gal b
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iii: Asp 258 metal interaction with gal b
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iv: Arginine 242 hydrogen bonds with ligand gal b, cation pi interactions with
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iv: Arginine 257 hydrogen bonds with ligand gal b, cation pi interactions with
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trp 95
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trp 110
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v: His 245 has metal interactions with Gal b
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v: His 260 has metal interactions with Gal b
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vi: Cys 136 and 94 disulfide bond and hydrogen bond with N-acetyl-d-
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vi: Cys 109 and 151 disulfide bond and hydrogen bond with N-acetyl-d-
glucosamine (GlcNAc)
glucosamine (GlcNAc)
 +
<scene name='86/861616/Important_amino_acids/2'>VIEW IMPORTANT AMINO ACIDS</scene>
== Structural highlights ==
== Structural highlights ==
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My protein is a epithelial adhesin protein binded to a Galactose beta 1-3 N-acetyl-D-Glucosamine, it contains 3 to 5 small alpha helices and a core of anti parralel beta sheets also known as the beta sandwich core. all of the important catalytic amino acids bind to the ligand by hydrogen bonds with the ligand itself or metal interaction with Ca+ its also contains a disulfide bond binding two loops together that are crucial in ligand affinity. It also contains two loops connected by a disulfide bond that play a key role in ligand affinity when these are changed the protien often accepts a different carbohydrate ligand
+
My protein is a epithelial adhesin protein bonded to a Galactose beta 1-3 N-acetyl-D-Glucosamine, it contains 3 to 5 small alpha helices and a core of anti parralel beta sheets also known as the beta sandwich core. all of the important catalytic amino acids bind to the ligand by hydrogen bonds with the ligand itself or metal interaction with Ca+ its also contains a disulfide bond binding two loops together that are crucial in ligand affinity. It also contains two loops connected by a disulfide bond that play a key role in ligand affinity when these are changed the protien often accepts a different carbohydrate ligand
== Other important features ==
== Other important features ==

Revision as of 16:47, 7 December 2020

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.
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