دورية أكاديمية
أعرض في EDS

Tracking Disordered Extracellular Domains of Membrane Proteins in the Cell with Cu(II)-Based Spin Labels.

التفاصيل البيبلوغرافية
العنوان: Tracking Disordered Extracellular Domains of Membrane Proteins in the Cell with Cu(II)-Based Spin Labels.
المؤلفون: Meron S; The Department of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar-Ilan University, Ramat-Gan 529002, Israel., Peleg S; The Department of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar-Ilan University, Ramat-Gan 529002, Israel., Shenberger Y; The Department of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar-Ilan University, Ramat-Gan 529002, Israel., Hofmann L; The Department of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar-Ilan University, Ramat-Gan 529002, Israel., Gevorkyan-Airapetov L; The Department of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar-Ilan University, Ramat-Gan 529002, Israel., Ruthstein S; The Department of Chemistry and the Institute of Nanotechnology and Advanced Materials, Faculty of Exact Sciences, Bar-Ilan University, Ramat-Gan 529002, Israel.
المصدر: The journal of physical chemistry. B [J Phys Chem B] 2024 Sep 19; Vol. 128 (37), pp. 8908-8914. Date of Electronic Publication: 2024 Sep 04.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 101157530 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5207 (Electronic) Linking ISSN: 15205207 NLM ISO Abbreviation: J Phys Chem B Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, D.C. : American Chemical Society, c1997-
مواضيع طبية MeSH: Copper*/chemistry , Spin Labels* , Copper Transporter 1*/metabolism , Copper Transporter 1*/chemistry, Humans ; Electron Spin Resonance Spectroscopy ; Protein Domains ; Animals ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism
مستخلص: In-cell electron paramagnetic resonance (EPR) spectroscopy experiments provide high-resolution data about conformational changes of proteins within the cell. However, one of the limitations of EPR is the requisite of stable paramagnetic centers in a reducing environment. We recently showed that histidine-rich sites in proteins hold a high affinity to Cu(II) ions complexed with a chelator. Using a chelator prevents the reduction of Cu(II) ions. Moreover, this spin-labeling methodology can be performed within the native cellular environment on any overexpressed protein without protein purification and delivery to the cell. Herein, we use this novel methodology to gain spatial information on the extracellular domain of the human copper transporter, hCtr1. Limited structural information on the transmembrane domain of the human Ctr1 (hCtr1) was obtained using X-ray crystallography and cryo-EM. However, these structures are missing information on the disordered extracellular domains of hCtr1. Extracellular domains are sensing or interacting with the environment outside of the cell and therefore play an essential role in any transmembrane protein. Especially in hCtr1, the extracellular domain functions as a gating mechanism for copper ions. Here, we performed EPR experiments revealing structural information about the extracellular N-terminal domain of the full-length hCtr1 in vitro and in situ in insect cells and cell membrane fragments. The comparison revealed that the extracellular domains of the in situ and native membrane hCtr1 are further apart than the structure of the purified protein. These method-related differences highlight the significance of studying membrane proteins in their native environment.
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المشرفين على المادة: 789U1901C5 (Copper)
0 (Spin Labels)
0 (Copper Transporter 1)
0 (SLC31A1 protein, human)
0 (Membrane Proteins)
تواريخ الأحداث: Date Created: 20240904 Date Completed: 20240919 Latest Revision: 20240926
رمز التحديث: 20240926
مُعرف محوري في PubMed: PMC11421077
DOI: 10.1021/acs.jpcb.4c03676
PMID: 39231533
قاعدة البيانات: MEDLINE
الوصف
تدمد:1520-5207
DOI:10.1021/acs.jpcb.4c03676