1w0t: Difference between revisions

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[[Image:1w0t.gif|left|200px]]
[[Image:1w0t.gif|left|200px]]


{{Structure
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The line below this paragraph, containing "STRUCTURE_1w0t", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|DOMAIN=
{{STRUCTURE_1w0t| PDB=1w0t  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w0t OCA], [http://www.ebi.ac.uk/pdbsum/1w0t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w0t RCSB]</span>
}}


'''HTRF1 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.'''
'''HTRF1 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.'''
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[[Category: Fairall, L.]]
[[Category: Fairall, L.]]
[[Category: Rhodes, D.]]
[[Category: Rhodes, D.]]
[[Category: adp-ribosylation]]
[[Category: Adp-ribosylation]]
[[Category: cell cycle]]
[[Category: Cell cycle]]
[[Category: chromosomal protein]]
[[Category: Chromosomal protein]]
[[Category: dna-binding protein]]
[[Category: Dna-binding protein]]
[[Category: homeodomain]]
[[Category: Homeodomain]]
[[Category: mitosis]]
[[Category: Mitosis]]
[[Category: nuclear protein]]
[[Category: Nuclear protein]]
[[Category: phosphorylation]]
[[Category: Phosphorylation]]
[[Category: telomere]]
[[Category: Telomere]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:00:18 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:29:33 2008''

Revision as of 13:00, 3 May 2008

File:1w0t.gif

Template:STRUCTURE 1w0t

HTRF1 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.


OverviewOverview

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.

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 Sat May 3 13:00:18 2008

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