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The dynamic nature of the VDAC1 channels in bilayers: human VDAC1 at 3.3 Angstrom resolution

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Protein Data Bank Japan2024-01-17 更新2026-03-21 收录
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https://pdbj.org/mine/summary/6g73
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The dynamic nature of the VDAC1 channels in bilayers: human VDAC1 at 3.3 Angstrom resolution Descriptor: 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE, Voltage-dependent anion-selective channel protein 1 Authors: Razeto, A, Gribbon, P, Loew, C. Deposit date: 2018-04-04 Release date: 2019-04-24 Last modified: 2024-01-17 Method: X-RAY DIFFRACTION (3.27 Å) Cite: The dynamic nature of the VDAC1 channels in bilayers as revealed by two crystal structures of the human isoform in bicelles at 2.7 and 3.3 Angstrom resolution: implications for VDAC1 voltage-dependent mechanism and for its oligomerization To Be Published
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2018-04-04
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