1ign
From Proteopedia
OCA (Talk | contribs)
(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 ...)
Next diff →
Revision as of 15:15, 20 November 2007
|
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
Page seeded by OCA on Tue Nov 20 17:23:07 2007
