1w0t: Difference between revisions

Revision as of 23:48, 27 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:1w0t.png

Template:STRUCTURE 1w0t

HTRF1 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.HTRF1 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.

Template:ABSTRACT PUBMED 15608617

About this StructureAbout this Structure

1W0T is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

How the human telomeric proteins TRF1 and TRF2 recognize telomeric DNA: a view from high-resolution crystal structures., Court R, Chapman L, Fairall L, Rhodes D, EMBO Rep. 2005 Jan;6(1):39-45. PMID:15608617

Page seeded by OCA on Sun Jul 27 23:48:06 2008

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

OCA

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-[[Image:1w0t.gif|left|200px]]
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 {{STRUCTURE_1w0t|  PDB=1w0t  |  SCENE=  }}
-'''HTRF1 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.'''
+===HTRF1 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.===
-==Overview==
+<!--
-Human telomeres consist of tandem arrays of TTAGGG sequence repeats that are specifically bound by two proteins, TRF1 and TRF2. They bind to DNA as preformed homodimers and have the same architecture in which the DNA-binding domains (Dbds) form independent structural units. Despite these similarities, TRF1 and TRF2 have different functions at telomeres. The X-ray crystal structures of both TRF1- and TRF2-Dbds in complex with telomeric DNA (2.0 and 1.8 angstroms resolution, respectively) show that they recognize the same TAGGGTT binding site by means of homeodomains, as does the yeast telomeric protein Rap1p. Two of the three G-C base pairs that characterize telomeric repeats are recognized specifically and an unusually large number of water molecules mediate protein-DNA interactions. The binding of the TRF2-Dbd to the DNA double helix shows no distortions that would account for the promotion of t-loops in which TRF2 has been implicated.
+The line below this paragraph, {{ABSTRACT_PUBMED_15608617}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15608617 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15608617}}
 ==About this Structure==
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 [[Category: Phosphorylation]]
 [[Category: Telomere]]
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