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

Paper ID Volume ID Publish Year Pages File Format Full-Text
15166 1384 2013 4 PDF Available
Title
Computational determination of the orientation of a heat repeat-like domain of DNA-PKcs
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.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Computational determination of orientation of heat repeat domain of DNA-PKcs. ► Presentation of structural model for heat repeat domain to enable design of experiments. ► Adaption of EM-Fold to work with X-ray density maps.

Keywords
Computational structure prediction; Medium resolution density maps
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Computational determination of the orientation of a heat repeat-like domain of DNA-PKcs
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Publisher
Database: Elsevier - ScienceDirect
Journal: Computational Biology and Chemistry - Volume 42, February 2013, Pages 1–4
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
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