Here, we propose to use this method to predict protein regions involved in the binding of nucleic acids. We have used the OB-fold, a motif known to promote protein-nucleic acid interactions, to validate our approach.#We have tested the method using this well-characterized nucleic acid binding...
The widespread oligonucleotide/oligosaccharide-binding (OB)-fold recognizes diverse substrates from sugars to nucleic acids and proteins, and plays key roles in genome maintenance, transcription, translation, and tRNA metabolism. OB-containing bacterial
Using dynamics-based comparisons to predict nucleic acid binding sites in proteins: an application to OB-fold domains. Motivation: We have previously demonstrated that proteins may be aligned not only by sequence or structural homology, but also using their dynamical proper... A Zen,CD Chiara,A ...
We find that the BRCT domain is required in its entirety for effective nick sealing and AMP-dependent supercoil relaxation. 展开 关键词: Escherichia coli Crystallography, X-Ray DNA Mutational Analysis Base Sequence Molecular Conformation Nucleic Acid Conformation Protein Structure, Tertiary Sequence ...
Orchestrating nucleic acid–protein interactions at chromosome ends: telomerase mechanisms come into focus Neal F. Lue Chantal Autexier Nature Structural & Molecular Biology (2023) Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase Nikita M. Shepelev Sofia S...
The OB fold indentation, which usually participates in nucleic acid or peptide binding is buried at the core of the OB2 dimer and is therefore not accessible for such interactions. Indeed, biochemical studies show that this domain does not associate with sstDNA or Stn1. The data presented ...
However, decreasing the length of apoB from apoB-42 to apoB-28 resulted in 2.6-fold increased binding. Further decrease in length from apoB-28 to apoB-17 resulted in another 2-fold increased binding to MTP. These studies indicated that the binding of apoB to MTP decreases with increases...
A domain analysis revealed the presence of one OB fold that corre- sponds to OB1 (Fig. 1D). Although both OB folds of the human POT1 possess ssDNA binding capacity, OB1 is indispensible for human POT1 binding to ssDNA. The C-terminus of human POT1 is responsible for associating ...
(http://www.ebi.ac.uk/dali/interactive.html) (Holm and Sander, 1998, Nucleic Acids Res 26, 316-319). Thus, it is easy to identify, for any OB-fold protein (or any OB-fold domain), the amino acids involved in the binding site and corresponding to the Sac7d amino acids mentioned ...
Accordingly, the present invention also relates to the identification of a nucleic acid having a nucleotide sequence selected from the sequences of FIG. 1 (SEQ ID NO:1) and FIG. 2 (SEQ ID NO:3) herein, and degenerate variants, allelic variations, and like cognate molecules. A nucleic ...