1ymo: Difference between revisions
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|PDB= 1ymo |SIZE=350|CAPTION= <scene name='initialview01'>1ymo</scene> | |PDB= 1ymo |SIZE=350|CAPTION= <scene name='initialview01'>1ymo</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=C:CYTIDINE-5'-MONOPHOSPHATE'>C</scene>, <scene name='pdbligand=G:GUANOSINE-5'-MONOPHOSPHATE'>G</scene>, <scene name='pdbligand=U:URIDINE-5'-MONOPHOSPHATE'>U</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<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.ebi.ac.uk/pdbsum/1ymo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ymo RCSB]</span> | |||
}} | }} | ||
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[[Category: Feigon, J.]] | [[Category: Feigon, J.]] | ||
[[Category: Theimer, C A.]] | [[Category: Theimer, C A.]] | ||
[[Category: hoogsteen]] | [[Category: hoogsteen,triplex]] | ||
[[Category: non-canonical]] | [[Category: non-canonical]] | ||
[[Category: pseudoknot]] | [[Category: pseudoknot]] | ||
[[Category: tertiary structure]] | [[Category: tertiary structure]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:13:21 2008'' | ||
Revision as of 01:13, 31 March 2008
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| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the P2b-P3 pseudoknot from human telomerase RNA
OverviewOverview
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 StructureAbout this Structure
1YMO is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
ReferenceReference
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
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