Sandbox GGC9

From Proteopedia

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=2m9v=
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==Name of your Protein==
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==Structure of Saccharomyces cerevisiae Est3 protein==
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<StructureSection load='3VEV' size='340' side='right' caption='Caption for this structure' scene=''>
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<StructureSection load='2m9v' size='340' side='right' caption='[[2m9v]], [[NMR_Ensembles_of_Models | 20 NMR models]]' 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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This is a default text for your page '''Sandbox GGC9'''. 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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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI:10.1073/pnas.1316453111</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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== Introduction ==
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Telomerase is essential for continuous cellular proliferation. Substantial insights have come from studies of budding yeast telomerase. In cells that lack telomerase, gradual erosion due to incomplete replication of duplex telomeric DNA leads to an eventual Block to cellular proliferation.<ref>DOI:10.1073/pnas.1316453111</ref>
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== Function ==
== Function ==
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A single pathway for telomere replication in the yeast Saccharomyces cerevisiae <ref>DOI:10.1016/s0960-9822(00)00562-5</ref>
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They have been studies about individual functions of the components of the S. cerevisiae telomerase.<ref>10.1093/nar/gkp1173</ref>
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Component of telomerase complex involved in telomere replication. Stimulates RNA/DNA heteroduplex unwinding which favors the telomere replication by the telomerase.<ref>DOI:10.1073/pnas.1316453111</ref>
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Est3 protein surface has an important opening up in the structurally similar human TPP1 protein. <ref>DOI:10.1073/pnas.1316453111</ref>
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== Disease ==
== Disease ==
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Saccharomyces cerevisiae is a species of yeast that is known in baking and brewing. Also, it is used as a probiotic in humans but it very uncommon infection in humans.<ref>https://doi.org/10.1086/429916</ref>
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== Relevance ==
== Relevance ==
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Studies have found Est3 adopts OB-fold with certain distinctive features. In most cases, the most notable discrepancy between Est and other OB-fold protein is OB-fold ligand-binding.<ref>DOI:10.1073/pnas.1316453111</ref>
 
== Structural highlights ==
== Structural highlights ==
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Deletion of 12 N-terminal residues, found to constitute this flexible region. The mutagenesis of the putative nonconserved surface cysteine residues (Cys64, Cys76, Cys109, and Cys142) which are identified as Cys 142Ser<ref>DOI:10.1073/pnas.1316453111</ref>
 
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This is <scene name='75/752271/2f6a/2'>2f6a
 
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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.
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 15:35, 10 February 2021

Name of your Protein

Caption for this structure

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References

  1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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