1ign
From Proteopedia
(New page: 200px<br /><applet load="1ign" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ign, resolution 2.250Å" /> '''DNA-BINDING DOMAIN ...) |
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| - | [[Image:1ign.gif|left|200px]]<br /><applet load="1ign" size=" | + | [[Image:1ign.gif|left|200px]]<br /><applet load="1ign" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ign, resolution 2.250Å" /> | caption="1ign, resolution 2.250Å" /> | ||
'''DNA-BINDING DOMAIN OF RAP1 IN COMPLEX WITH TELOMERIC DNA SITE'''<br /> | '''DNA-BINDING DOMAIN OF RAP1 IN COMPLEX WITH TELOMERIC DNA SITE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Telomeres, the nucleoprotein complexes at the ends of eukaryotic | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1IGN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http:// | + | 1IGN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IGN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: yeast]] | [[Category: yeast]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:43 2008'' |
Revision as of 11:11, 21 February 2008
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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.
About this Structure
1IGN is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA., Konig P, Giraldo R, Chapman L, Rhodes D, Cell. 1996 Apr 5;85(1):125-36. PMID:8620531
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