1ign | pdb_00001ign
DNA-BINDING DOMAIN OF RAP1 IN COMPLEX WITH TELOMERIC DNA SITE
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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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