3U90
apoferritin: complex with SDS
3U90 の概要
エントリーDOI | 10.2210/pdb3u90/pdb |
関連するPDBエントリー | 3F32 |
分子名称 | Ferritin light chain, DODECYL SULFATE, CADMIUM ION, ... (4 entities in total) |
機能のキーワード | four helix bundle, iron-binding protein, intracellular protein, metal binding protein |
由来する生物種 | Equus caballus (horse) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 21262.94 |
構造登録者 | Liu, R.,Bu, W.,Xi, J.,Mortazavi, S.R.,Cheung-Lau, J.C.,Dmochowski, I.J.,Loll, P.J. (登録日: 2011-10-17, 公開日: 2012-04-25, 最終更新日: 2023-09-13) |
主引用文献 | Liu, R.,Bu, W.,Xi, J.,Mortazavi, S.R.,Cheung-Lau, J.C.,Dmochowski, I.J.,Loll, P.J. Beyond the detergent effect: a binding site for sodium dodecyl sulfate (SDS) in mammalian apoferritin. Acta Crystallogr.,Sect.D, 68:497-504, 2012 Cited by PubMed Abstract: 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 µM 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. PubMed: 22525747DOI: 10.1107/S0907444912002740 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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