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[[Image:1ymo.gif|left|200px]]
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{{STRUCTURE_1ymo|  PDB=1ymo  |  SCENE=  }}
'''Solution structure of the P2b-P3 pseudoknot from human telomerase RNA'''


==Solution structure of the P2b-P3 pseudoknot from human telomerase RNA==
<StructureSection load='1ymo' size='340' side='right'caption='[[1ymo]]' scene=''>
== Structural highlights ==
<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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<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>
</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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YMO OCA].
</div>
<div class="pdbe-citations 1ymo" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Telomerase 3D structures|Telomerase 3D structures]]
[[Category: Blois, C A.]]
== References ==
[[Category: Feigon, J.]]
<references/>
[[Category: Theimer, C A.]]
__TOC__
[[Category: Hoogsteen,triplex]]
</StructureSection>
[[Category: Non-canonical]]
[[Category: Homo sapiens]]
[[Category: Pseudoknot]]
[[Category: Large Structures]]
[[Category: Tertiary structure]]
[[Category: Blois CA]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:31:00 2008''
[[Category: Feigon J]]
[[Category: Theimer CA]]

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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