Journal article
Beyond the detergent effect: a binding site for sodium dodecyl sulfate (SDS) in mammalian apoferritin
Acta crystallographica. Section D, Biological crystallography., v 68(Pt 5), pp 497-504
01 May 2012
PMID: 22525747
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Using X-ray crystallography and isothermal titration calorimetry, we show that sodium dodecyl sulfate (SDS) binds specifically to a pre-formed internal cavity in horse-spleen apoferritin.
Although sodium dodecyl sulfate (SDS) is widely used as an anionic detergent, it can also exert specific pharmacological effects that are independent of the surfactant properties of the molecule. However, structural details of how proteins recognize SDS are scarce. Here, it is demonstrated that SDS binds specifically to a naturally occurring four-helix bundle protein: horse apoferritin. The X-ray crystal structure of the apoferritin–SDS complex was determined at a resolution of 1.9 Å and revealed that the SDS binds in an internal cavity that has previously been shown to recognize various general anesthetics. A dissociation constant of 24 ± 9 µ
M
at 293 K was determined by isothermal titration calorimetry. SDS binds in this cavity by bending its alkyl tail into a horseshoe shape; the charged SDS head group lies in the opening of the cavity at the protein surface. This crystal structure provides insights into the protein–SDS interactions that give rise to binding and may prove useful in the design of novel SDS-like ligands for some proteins.
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Details
- Title
- Beyond the detergent effect: a binding site for sodium dodecyl sulfate (SDS) in mammalian apoferritin
- Creators
- Renyu Liu - Department of Anesthesia and Critical CareWeiming Bu - Department of Anesthesia and Critical CareJin Xi - Department of Anesthesia and Critical CareShirin R Mortazavi - Department of Biochemistry and Molecular BiologyJasmina C Cheung-Lau - Department of Anesthesia and Critical CareIvan J Dmochowski - Department of ChemistryPatrick J Loll - Department of Biochemistry and Molecular Biology
- Publication Details
- Acta crystallographica. Section D, Biological crystallography., v 68(Pt 5), pp 497-504
- Publisher
- International Union of Crystallography
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000303159000001
- Scopus ID
- 2-s2.0-84860305334
- Other Identifier
- 991014878040404721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemical Research Methods
- Biochemistry & Molecular Biology
- Biophysics
- Crystallography