This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2i46

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2i46.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2i46.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2i46| PDB=2i46 | SCENE= }}
{{STRUCTURE_2i46| PDB=2i46 | SCENE= }}
-
'''Crystal structure of human TPP1'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17237768}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17237768 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17237768}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Pot1 binding]]
[[Category: Pot1 binding]]
[[Category: Tpp1]]
[[Category: Tpp1]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:02:44 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:51:58 2008''

Revision as of 05:52, 28 July 2008

Image:2i46.png

Template:STRUCTURE 2i46

Crystal structure of human TPP1

Template:ABSTRACT PUBMED 17237768

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 Mon Jul 28 08:51:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2i46"
Personal tools