Sandbox GGC9

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== Structural highlights ==
== Structural highlights ==
 +
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>
 +
This is <scene name='75/752271/2f6a/2'>2f6a
This is <scene name='75/752271/2f6a/2'>2f6a
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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>
+
</StructureSection>
</StructureSection>
== References ==
== References ==
<references/>
<references/>

Revision as of 19:58, 16 November 2020

2m9v

Structure of Saccharomyces cerevisiae Est3 protein

Drag the structure with the mouse to rotate

References

  1. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:http://dx.doi.org/10.1073/pnas.1316453111
  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
  3. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:http://dx.doi.org/10.1073/pnas.1316453111
  4. ↑ doi: https://dx.doi.org/10.1016/s0960-9822(00)00562-5
  5. ↑ 10.1093/nar/gkp1173
  6. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:http://dx.doi.org/10.1073/pnas.1316453111
  7. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:http://dx.doi.org/10.1073/pnas.1316453111
  8. ↑ https://doi.org/10.1086/429916
  9. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:http://dx.doi.org/10.1073/pnas.1316453111
  10. ↑ Rao T, Lubin JW, Armstrong GS, Tucey TM, Lundblad V, Wuttke DS. Structure of Est3 reveals a bimodal surface with differential roles in telomere replication. Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):214-8. doi: 10.1073/pnas.1316453111. , Epub 2013 Dec 16. PMID:24344315 doi:http://dx.doi.org/10.1073/pnas.1316453111
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