1h6o

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[[Image:1h6o.gif|left|200px]]
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{{STRUCTURE_1h6o| PDB=1h6o | SCENE= }}
{{STRUCTURE_1h6o| PDB=1h6o | SCENE= }}
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'''DIMERISATION DOMAIN FROM HUMAN TRF1'''
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===DIMERISATION DOMAIN FROM HUMAN TRF1===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11545737 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11545737}}
==About this Structure==
==About this Structure==
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[[Category: Trf1]]
[[Category: Trf1]]
[[Category: Trfh]]
[[Category: Trfh]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:30:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:42:52 2008''

Revision as of 03:42, 1 July 2008

Template:STRUCTURE 1h6o

DIMERISATION DOMAIN FROM HUMAN TRF1

Template:ABSTRACT PUBMED 11545737

About this Structure

1H6O 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

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