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~~'''~~DNA-BINDING DOMAIN OF RAP1 IN COMPLEX WITH TELOMERIC DNA SITE~~'''~~

===DNA-BINDING DOMAIN OF RAP1 IN COMPLEX WITH TELOMERIC DNA SITE===

~~==Overview==~~

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~~Telomeres~~, the ~~nucleoprotein complexes~~ at ~~the ends of eukaryotic chromosomes, are essential for chromosome stability~~. ~~In the yeast S~~. ~~cerevisiae~~, ~~telomeric DNA~~ is ~~bound in a sequence-specific manner by RAP1, a multifunctional protein also involved in transcriptional regulation. Here we report~~ the ~~crystal structure of the DNA-binding domain of RAP1 in complex with telomeric DNA site at 2~~.25 A resolution. The protein contains two similar domains that bind DNA in a tandem orientation, recognizing a tandemly repeated DNA sequence. The domains are structurally related to the homeodomain and the proto-~~oncogene Myb, but show novel features in their DNA~~-binding mode. A structured linker between the domains and a long C-terminal tail contribute to the binding specificity. This structure provides insight into the recognition of the conserved telomeric DNA sequences by a protein.

The line below this paragraph, {{ABSTRACT_PUBMED_8620531}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8620531 is the PubMed ID number.

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==About this Structure==

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[[Category: Rhodes, D.]]

[[Category: Rap1,yeast,telomeres,homoeodomain]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 19~~:58:32 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:41:38 2008''

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-[[Image:1ign.gif|left|200px]]
+{{Seed}}
+[[Image:1ign.png|left|200px]]
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 {{STRUCTURE_1ign|  PDB=1ign  |  SCENE=  }}
-'''DNA-BINDING DOMAIN OF RAP1 IN COMPLEX WITH TELOMERIC DNA SITE'''
+===DNA-BINDING DOMAIN OF RAP1 IN COMPLEX WITH TELOMERIC DNA SITE===
-==Overview==
+<!--
-Telomeres, the nucleoprotein complexes at the ends of eukaryotic chromosomes, are essential for chromosome stability. In the yeast S. cerevisiae, telomeric DNA is bound in a sequence-specific manner by RAP1, a multifunctional protein also involved in transcriptional regulation. Here we report the crystal structure of the DNA-binding domain of RAP1 in complex with telomeric DNA site at 2.25 A resolution. The protein contains two similar domains that bind DNA in a tandem orientation, recognizing a tandemly repeated DNA sequence. The domains are structurally related to the homeodomain and the proto-oncogene Myb, but show novel features in their DNA-binding mode. A structured linker between the domains and a long C-terminal tail contribute to the binding specificity. This structure provides insight into the recognition of the conserved telomeric DNA sequences by a protein.
+The line below this paragraph, {{ABSTRACT_PUBMED_8620531}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8620531 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8620531}}
 ==About this Structure==
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 [[Category: Rhodes, D.]]
 [[Category: Rap1,yeast,telomeres,homoeodomain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:58:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:41:38 2008''