Structural features of Dnase1L3 responsible for serum antigen clearance

Jon J. McCord; Minal Engavale; Elahe Masoumzadeh; Johanna Villarreal; Britney Mapp; Michael P. Latham; Peter A. Keyel; R. Bryan Sutton

doi:10.1038/s42003-022-03755-5

Communications Biology (Aug 2022)

Structural features of Dnase1L3 responsible for serum antigen clearance

Jon J. McCord,
Minal Engavale,
Elahe Masoumzadeh,
Johanna Villarreal,
Britney Mapp,
Michael P. Latham,
Peter A. Keyel,
R. Bryan Sutton

Affiliations

Jon J. McCord: Texas Tech University Health Sciences Center, Dept of Cell Physiology and Molecular Biophysics
Minal Engavale: Texas Tech University, Dept. of Biological Sciences
Elahe Masoumzadeh: Texas Tech University, Dept. of Chemistry & Biochemistry
Johanna Villarreal: Texas Tech University Health Sciences Center, Dept of Cell Physiology and Molecular Biophysics
Britney Mapp: Texas Tech University, Dept. of Biological Sciences
Michael P. Latham: Texas Tech University, Dept. of Chemistry & Biochemistry
Peter A. Keyel: Texas Tech University, Dept. of Biological Sciences
R. Bryan Sutton: Texas Tech University Health Sciences Center, Dept of Cell Physiology and Molecular Biophysics

DOI: https://doi.org/10.1038/s42003-022-03755-5
Journal volume & issue: Vol. 5, no. 1
pp. 1 – 13

Abstract

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Biophysical, structural, and functional characterization of Dnase1L3 reveals differences in DNA binding and degradation mechanisms between Dnase1 and Dnase1L3 facilitated by Dnase1L3’s intrinsically disordered C-terminal domain.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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