1ymo: Difference between revisions

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[[Image:1ymo.png|left|200px]]


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==Solution structure of the P2b-P3 pseudoknot from human telomerase RNA==
The line below this paragraph, containing "STRUCTURE_1ymo", creates the "Structure Box" on the page.
<StructureSection load='1ymo' size='340' side='right'caption='[[1ymo]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ymo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YMO FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ymo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ymo OCA], [https://pdbe.org/1ymo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ymo RCSB], [https://www.ebi.ac.uk/pdbsum/1ymo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ymo ProSAT]</span></td></tr>
{{STRUCTURE_1ymo|  PDB=1ymo  |  SCENE=  }}
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Human telomerase contains a 451 nt RNA (hTR) and several proteins, including a specialized reverse transcriptase (hTERT). The 5' half of hTR comprises the pseudoknot (core) domain, which includes the RNA template for telomere synthesis and a highly conserved pseudoknot that is required for telomerase activity. The solution structure of this essential pseudoknot, presented here, reveals an extended triple helix surrounding the helical junction. The network of tertiary interactions explains the phylogenetic sequence conservation and existing human and mouse TR functional studies as well as mutations linked to disease. Thermodynamic stability, dimerization potential, and telomerase activity of mutant RNAs that alter the tertiary contacts were investigated. Telomerase activity is strongly correlated with tertiary structure stability, whereas there is no correlation with dimerization potential of the pseudoknot. These studies reveal that a conserved pseudoknot tertiary structure is required for telomerase activity.


===Solution structure of the P2b-P3 pseudoknot from human telomerase RNA===
Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function.,Theimer CA, Blois CA, Feigon J Mol Cell. 2005 Mar 4;17(5):671-82. PMID:15749017<ref>PMID:15749017</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ymo" style="background-color:#fffaf0;"></div>


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==See Also==
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*[[Telomerase 3D structures|Telomerase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15749017 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_15749017}}
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</StructureSection>
==About this Structure==
[[Category: Homo sapiens]]
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YMO OCA].
[[Category: Large Structures]]
 
[[Category: Blois CA]]
==Reference==
[[Category: Feigon J]]
Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function., Theimer CA, Blois CA, Feigon J, Mol Cell. 2005 Mar 4;17(5):671-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15749017 15749017]
[[Category: Theimer CA]]
[[Category: Blois, C A.]]
[[Category: Feigon, J.]]
[[Category: Theimer, C A.]]
[[Category: Hoogsteen,triplex]]
[[Category: Non-canonical]]
[[Category: Pseudoknot]]
[[Category: Tertiary structure]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:00:39 2008''

Latest revision as of 17:17, 29 November 2023

Solution structure of the P2b-P3 pseudoknot from human telomerase RNASolution structure of the P2b-P3 pseudoknot from human telomerase RNA

Structural highlights

1ymo is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Human telomerase contains a 451 nt RNA (hTR) and several proteins, including a specialized reverse transcriptase (hTERT). The 5' half of hTR comprises the pseudoknot (core) domain, which includes the RNA template for telomere synthesis and a highly conserved pseudoknot that is required for telomerase activity. The solution structure of this essential pseudoknot, presented here, reveals an extended triple helix surrounding the helical junction. The network of tertiary interactions explains the phylogenetic sequence conservation and existing human and mouse TR functional studies as well as mutations linked to disease. Thermodynamic stability, dimerization potential, and telomerase activity of mutant RNAs that alter the tertiary contacts were investigated. Telomerase activity is strongly correlated with tertiary structure stability, whereas there is no correlation with dimerization potential of the pseudoknot. These studies reveal that a conserved pseudoknot tertiary structure is required for telomerase activity.

Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function.,Theimer CA, Blois CA, Feigon J Mol Cell. 2005 Mar 4;17(5):671-82. PMID:15749017[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Theimer CA, Blois CA, Feigon J. Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function. Mol Cell. 2005 Mar 4;17(5):671-82. PMID:15749017 doi:10.1016/j.molcel.2005.01.017
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