1ymo: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ymo]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YMO FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ymo]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YMO FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k96|2k96]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2k96|2k96]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ymo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ymo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ymo RCSB], [http://www.ebi.ac.uk/pdbsum/1ymo PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ymo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ymo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ymo RCSB], [http://www.ebi.ac.uk/pdbsum/1ymo PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Telomerase|Telomerase]] | *[[Telomerase 3D structures|Telomerase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Blois, C A | [[Category: Blois, C A]] | ||
[[Category: Feigon, J | [[Category: Feigon, J]] | ||
[[Category: Theimer, C A | [[Category: Theimer, C A]] | ||
[[Category: Hoogsteen]] | [[Category: Hoogsteen]] | ||
[[Category: Non-canonical]] | [[Category: Non-canonical]] | ||
Revision as of 13:53, 25 January 2015
Solution structure of the P2b-P3 pseudoknot from human telomerase RNASolution structure of the P2b-P3 pseudoknot from human telomerase RNA
Structural highlights
Publication Abstract from PubMedHuman 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 AlsoReferences
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