2i46

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[[Image:2i46.gif|left|200px]]
[[Image:2i46.gif|left|200px]]
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{{Structure
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|PDB= 2i46 |SIZE=350|CAPTION= <scene name='initialview01'>2i46</scene>, resolution 2.7&Aring;
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The line below this paragraph, containing "STRUCTURE_2i46", creates the "Structure Box" on the page.
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|GENE= ACD, PIP1, PTOP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_2i46| PDB=2i46 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i46 OCA], [http://www.ebi.ac.uk/pdbsum/2i46 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i46 RCSB]</span>
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'''Crystal structure of human TPP1'''
'''Crystal structure of human TPP1'''
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[[Category: Yang, Y T.]]
[[Category: Yang, Y T.]]
[[Category: Zaug, A J.]]
[[Category: Zaug, A J.]]
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[[Category: ob fold]]
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[[Category: Ob fold]]
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[[Category: pot1 binding]]
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[[Category: Pot1 binding]]
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[[Category: tpp1]]
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[[Category: Tpp1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:02:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:39:24 2008''
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Revision as of 04:02, 4 May 2008

Image:2i46.gif

Template:STRUCTURE 2i46

Crystal structure of human TPP1


Overview

Telomeres were originally defined as chromosome caps that prevent the natural ends of linear chromosomes from undergoing deleterious degradation and fusion events. POT1 (protection of telomeres) protein binds the single-stranded G-rich DNA overhangs at human chromosome ends and suppresses unwanted DNA repair activities. TPP1 is a previously identified binding partner of POT1 that has been proposed to form part of a six-protein shelterin complex at telomeres. Here, the crystal structure of a domain of human TPP1 reveals an oligonucleotide/oligosaccharide-binding fold that is structurally similar to the beta-subunit of the telomere end-binding protein of a ciliated protozoan, suggesting that TPP1 is the missing beta-subunit of human POT1 protein. Telomeric DNA end-binding proteins have generally been found to inhibit rather than stimulate the action of the chromosome end-replicating enzyme, telomerase. In contrast, we find that TPP1 and POT1 form a complex with telomeric DNA that increases the activity and processivity of the human telomerase core enzyme. We propose that POT1-TPP1 switches from inhibiting telomerase access to the telomere, as a component of shelterin, to serving as a processivity factor for telomerase during telomere extension.

About this Structure

2I46 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The POT1-TPP1 telomere complex is a telomerase processivity factor., Wang F, Podell ER, Zaug AJ, Yang Y, Baciu P, Cech TR, Lei M, Nature. 2007 Feb 1;445(7127):506-10. Epub 2007 Jan 21. PMID:17237768 Page seeded by OCA on Sun May 4 07:02:44 2008

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