1z31: Difference between revisions

Revision as of 07:22, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1z31.png

Template:STRUCTURE 1z31

The structure of an enzyme-activating fragment of human telomerase RNAThe structure of an enzyme-activating fragment of human telomerase RNA

Template:ABSTRACT PUBMED 15703438

About this StructureAbout this Structure

Full experimental information is available from OCA.

ReferenceReference

The structure of an enzyme-activating fragment of human telomerase RNA., Leeper TC, Varani G, RNA. 2005 Apr;11(4):394-403. Epub 2005 Feb 9. PMID:15703438

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''The structure of an enzyme-activating fragment of human telomerase RNA'''
+===The structure of an enzyme-activating fragment of human telomerase RNA===
-==Overview==
+<!--
-The ribonucleoprotein enzyme telomerase ensures the stability and fidelity of linear chromosome ends by elongating the telomeric DNA that is lost during each round of DNA replication. All telomerases contain a catalytic protein component homologous to viral reverse transcriptases (TERT) and an RNA (TR) that provides the template sequence, acts as the scaffold for ribonucleoprotein assembly, and activates the enzyme for catalysis. Vertebrate telomerase RNAs contain three highly conserved structural and functional domains: the template domain, the "CR4-CR5" or "activation" domain essential for activation of the enzymatic activity, and a 3'-terminal "box H/ACA"-homology domain responsible for ribonucleprotein assembly and maturation. Here we report the NMR structure of a functionally essential RNA structural element derived from the human telomerase RNA CR4-CR5 domain. This RNA, referred to as hTR J6, forms a stable hairpin interrupted by a single nucleotide bulge and an asymmetric internal loop. Previous work on telomerase has shown that deletion of the hTR J6 asymmetric internal loop results in an RNA incapable of binding the enzymatic protein component of the RNP and therefore an inactive RNP without telomerase activity. We demonstrate here that the J6 internal loop introduces a twist in the RNA structure that may position the entire domain into the catalytic site of the enzyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_15703438}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15703438 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15703438}}
 ==About this Structure==
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z31 OCA].
+Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z31 OCA].
 ==Reference==
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 [[Category: Residual dipolar coupling]]
 [[Category: Telomerase protein binding site]]
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