The Structure of Human DNase I Bound to Magnesium and Phosphate Ions Points to a Catalytic Mechanism Common to Members of the DNase I-like Superfamily

Goetz Parsiegla; Christophe Noguere; Lydia Santell; Robert Lazarus; Yves Bourne

doi:10.1021/bi300873f

Journal Articles Biochemistry Year : 2012

The Structure of Human DNase I Bound to Magnesium and Phosphate Ions Points to a Catalytic Mechanism Common to Members of the DNase I-like Superfamily

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Goetz Parsiegla

Function : Author

Bioénergétique et Ingénierie des Protéines

Christophe Noguere

Function : Author

Architecture et fonction des macromolécules biologiques

Lydia Santell

Function : Author

Genentech, Inc.

Robert Lazarus

Function : Author

Genentech, Inc.

Yves Bourne

Function : Author

Architecture et fonction des macromolécules biologiques

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Life Sciences [q-bio] Biochemistry, Molecular Biology

Yves Bourne : Connect in order to contact the contributor

https://hal-amu.archives-ouvertes.fr/hal-03533633

Submitted on : Tuesday, January 18, 2022-9:02:32 PM

Last modification on : Wednesday, February 8, 2023-5:11:22 PM

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hal-03533633 , version 1 (18-01-2022)

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HAL Id : hal-03533633 , version 1
DOI : 10.1021/bi300873f

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Goetz Parsiegla, Christophe Noguere, Lydia Santell, Robert Lazarus, Yves Bourne. The Structure of Human DNase I Bound to Magnesium and Phosphate Ions Points to a Catalytic Mechanism Common to Members of the DNase I-like Superfamily. Biochemistry, 2012, 51 (51), pp.10250-10258. ⟨10.1021/bi300873f⟩. ⟨hal-03533633⟩

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The Structure of Human DNase I Bound to Magnesium and Phosphate Ions Points to a Catalytic Mechanism Common to Members of the DNase I-like Superfamily

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