Computational determination of the orientation of a heat repeat-like domain of DNA-PKcs.

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Computational determination of the orientation of a heat repeat-like domain of DNA-PKcs.

Comput Biol Chem. 2013 Feb;42:1-4

Authors: Lindert S, Stewart PL, Meiler J

Abstract
DNA dependent protein kinase catalytic subunit (DNA-PKcs) is an important regulatory protein in non-homologous end joining a process used to repair DNA double strand breaks. Medium resolution structures both from cryoEM and X-ray crystallography show the general topology of the protein and positions of helices in parts of DNA-PKcs. EM-Fold, an algorithm developed for building protein models into medium resolution density maps has been used to generate models for the heat repeat-like "Ring structure" of the molecule. We were able to computationally corroborate placement of the N-terminus of the domain that supports a previously published hypothesis. Targeted experiments are suggested to test the model.

PMID: 23246775 [PubMed - in process]

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