4o26: Difference between revisions
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<StructureSection load='4o26' size='340' side='right' caption='[[4o26]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4o26' size='340' side='right' caption='[[4o26]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4o26]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O26 OCA]. <br> | <table><tr><td colspan='2'>[[4o26]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O26 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | ||
<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=4o26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o26 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o26 RCSB], [http://www.ebi.ac.uk/pdbsum/4o26 PDBsum]</span></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=4o26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o26 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o26 RCSB], [http://www.ebi.ac.uk/pdbsum/4o26 PDBsum]</span></td></tr> | ||
<table> | <table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Telomerase is a large ribonucleoprotein complex minimally composed of a catalytic telomerase reverse transcriptase (TERT) and an RNA component (TR) that provides the template for telomeric DNA synthesis. However, it remains unclear how TERT and TR assemble into a functional telomerase. Here we report the crystal structure of the conserved regions 4 and 5 (CR4/5) of TR in complex with the TR-binding domain (TRBD) of TERT from the teleost fish Oryzias latipes. The structure shows that CR4/5 adopts an L-shaped three-way-junction conformation with its two arms clamping onto TRBD. Both the sequence and conformation of CR4/5 are required for the interaction. Our structural and mutational analyses suggest that the observed CR4/5-TRBD recognition is common to most eukaryotes, and CR4/5 in vertebrate TR might have a similar role in telomerase regulation as that of stem-loop IV in Tetrahymena TR. | |||
Structural basis for protein-RNA recognition in telomerase.,Huang J, Brown AF, Wu J, Xue J, Bley CJ, Rand DP, Wu L, Zhang R, Chen JJ, Lei M Nat Struct Mol Biol. 2014 Jun;21(6):507-12. doi: 10.1038/nsmb.2819. Epub 2014 May, 4. PMID:24793650<ref>PMID:24793650</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Telomerase Reverse Transcriptase|Telomerase Reverse Transcriptase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:43, 18 June 2014
Crystal structure of the TRBD domain of TERT and the CR4/5 of TR
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