1h6p

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[[Image:1h6p.gif|left|200px]]<br /><applet load="1h6p" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1h6p.gif|left|200px]]
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caption="1h6p, resolution 2.20&Aring;" />
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'''DIMERISTION DOMAIN FROM HUMAN TRF2'''<br />
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{{Structure
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|PDB= 1h6p |SIZE=350|CAPTION= <scene name='initialview01'>1h6p</scene>, resolution 2.20&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''DIMERISTION DOMAIN FROM HUMAN TRF2'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1H6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H6P OCA].
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1H6P is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H6P OCA].
==Reference==
==Reference==
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Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2., Fairall L, Chapman L, Moss H, de Lange T, Rhodes D, Mol Cell. 2001 Aug;8(2):351-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11545737 11545737]
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Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2., Fairall L, Chapman L, Moss H, de Lange T, Rhodes D, Mol Cell. 2001 Aug;8(2):351-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11545737 11545737]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: trfh]]
[[Category: trfh]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:33:02 2008''

Revision as of 09:33, 20 March 2008

Image:1h6p.gif


PDB ID 1h6p

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



DIMERISTION DOMAIN FROM HUMAN TRF2


Overview

TRF1 and TRF2 are key components of vertebrate telomeres. They bind to double-stranded telomeric DNA as homodimers. Dimerization involves the TRF homology (TRFH) domain, which also mediates interactions with other telomeric proteins. The crystal structures of the dimerization domains from human TRF1 and TRF2 were determined at 2.9 and 2.2 A resolution, respectively. Despite a modest sequence identity, the two TRFH domains have the same entirely alpha-helical architecture, resembling a twisted horseshoe. The dimerization interfaces feature unique interactions that prevent heterodimerization. Mutational analysis of TRF1 corroborates the structural data and underscores the importance of the TRFH domain in dimerization, DNA binding, and telomere localization. A possible structural homology between the TRFH domain of fission yeast telomeric protein Taz1 with those of the vertebrate TRFs is suggested.

About this Structure

1H6P is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2., Fairall L, Chapman L, Moss H, de Lange T, Rhodes D, Mol Cell. 2001 Aug;8(2):351-61. PMID:11545737

Page seeded by OCA on Thu Mar 20 11:33:02 2008

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