1h6p: Difference between revisions

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[[Image:1h6p.~~gif~~|left|200px]]

[[Image:1h6p.png|left|200px]]

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~~'''~~DIMERISTION DOMAIN FROM HUMAN TRF2~~'''~~

===DIMERISTION DOMAIN FROM HUMAN TRF2===

~~==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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_11545737}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11545737 is the PubMed ID number.

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==About this Structure==

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[[Category: Trf2]]

[[Category: Trfh]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 18~~:30:10 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:42:52 2008''

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-[[Image:1h6p.gif|left|200px]]
+{{Seed}}
+[[Image:1h6p.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1h6p|  PDB=1h6p  |  SCENE=  }}
-'''DIMERISTION DOMAIN FROM HUMAN TRF2'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11545737}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11545737 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11545737}}
 ==About this Structure==
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 [[Category: Trf2]]
 [[Category: Trfh]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:30:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:42:52 2008''