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Solution Structure of the Cdc13 DNA-binding Domain in a Complex with Single-Stranded Telomeric DNA (DNA structure not modeled)Solution Structure of the Cdc13 DNA-binding Domain in a Complex with Single-Stranded Telomeric DNA (DNA structure not modeled)
Structural highlights
FunctionCDC13_YEAST Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG(1-3)] strand lengthening via interaction with EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomerase activity.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe essential Cdc13 protein in the yeast Saccharomyces cerevisiae is a single-stranded telomeric DNA binding protein required for chromosome end protection and telomere replication. Here we report the solution structure of the Cdc13 DNA binding domain in complex with telomeric DNA. The structure reveals the use of a single OB (oligonucleotide/oligosaccharide binding) fold augmented by an unusually large loop for DNA recognition. This OB fold is structurally similar to OB folds found in the ciliated protozoan telomere end-binding protein, although no sequence similarity is apparent between them. The common usage of an OB fold for telomeric DNA interaction demonstrates conservation of end-protection mechanisms among eukaryotes. Conserved structure for single-stranded telomeric DNA recognition.,Mitton-Fry RM, Anderson EM, Hughes TR, Lundblad V, Wuttke DS Science. 2002 Apr 5;296(5565):145-7. PMID:11935027[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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