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1
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Proc Natl Acad Sci U S A. 2001 Apr 24;98(9):4888-92. doi: 10.1073/pnas.051633098.
2
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3
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4
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5
Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1.探索视紫红质细胞质结构域中的暗态三级结构：通过半胱氨酸316与细胞质环1中工程化半胱氨酸之间自发形成的二硫键推断氨基酸之间的距离
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6
Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes upon light-activation.视紫红质中连接螺旋I和螺旋II胞质端的氨基酸序列55 - 75处的单半胱氨酸取代突变体：巯基及其衍生物的反应性确定了一种在光激活时会发生变化的三级结构。
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7
Solution NMR spectroscopy of [alpha -15N]lysine-labeled rhodopsin: The single peak observed in both conventional and TROSY-type HSQC spectra is ascribed to Lys-339 in the carboxyl-terminal peptide sequence.[α-¹⁵N]赖氨酸标记的视紫红质的溶液核磁共振光谱：在传统和TROSY型HSQC光谱中观察到的单峰归因于羧基末端肽序列中的Lys-339。
Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3452-7. doi: 10.1073/pnas.052713999.
8
Single-cysteine substitution mutants at amino acid positions 306-321 in rhodopsin, the sequence between the cytoplasmic end of helix VII and the palmitoylation sites: sulfhydryl reactivity and transducin activation reveal a tertiary structure.视紫红质中第306 - 321位氨基酸处的单半胱氨酸取代突变体，即螺旋VII胞质末端与棕榈酰化位点之间的序列：巯基反应性和转导素激活揭示了一种三级结构。
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9
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Biochemistry. 1999 Jun 22;38(25):7931-7. doi: 10.1021/bi9900121.
10
Tertiary interactions between transmembrane segments 3 and 5 near the cytoplasmic side of rhodopsin.
Biochemistry. 1999 Sep 14;38(37):12033-40. doi: 10.1021/bi9909492.

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本文引用的文献

1
The molar extinction of rhodopsin.视紫红质的摩尔消光系数。
J Gen Physiol. 1953 Nov 20;37(2):189-200. doi: 10.1085/jgp.37.2.189.
2
Crystal structure of rhodopsin: A G protein-coupled receptor.视紫红质的晶体结构：一种G蛋白偶联受体。
Science. 2000 Aug 4;289(5480):739-45. doi: 10.1126/science.289.5480.739.
3
Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure.自旋标记T4溶菌酶突变体的晶体结构：对根据结构解释电子顺磁共振光谱的意义。
Biochemistry. 2000 Jul 25;39(29):8396-405. doi: 10.1021/bi000604f.
4
Expression and purification of rhodopsin and its mutants from stable mammalian cell lines: application to NMR studies.来自稳定哺乳动物细胞系的视紫红质及其突变体的表达与纯化：在核磁共振研究中的应用
Biochem Soc Trans. 1999 Dec;27(6):950-5. doi: 10.1042/bst0270950.
5
NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: applicability of solution (19)F NMR.核磁共振光谱法在哺乳动物视紫红质光诱导结构变化研究中的应用：溶液（19）F核磁共振的适用性
Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13744-9. doi: 10.1073/pnas.96.24.13744.
6
Structure and function in rhodopsin: effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase.视紫红质的结构与功能：视紫红质胞质面二硫键交联对视紫红质激酶激活转导素及磷酸化作用的影响
Biochemistry. 1999 Sep 28;38(39):12893-8. doi: 10.1021/bi9912443.
7
Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: a site-directed spin-labeling study.视紫红质中连接螺旋I和螺旋II的59 - 75序列的结构特征及光依赖性变化：一项定点自旋标记研究。
Biochemistry. 1999 Jun 22;38(25):7945-9. doi: 10.1021/bi990014l.
8
Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes upon light-activation.视紫红质中连接螺旋I和螺旋II胞质端的氨基酸序列55 - 75处的单半胱氨酸取代突变体：巯基及其衍生物的反应性确定了一种在光激活时会发生变化的三级结构。
Biochemistry. 1999 Jun 22;38(25):7938-44. doi: 10.1021/bi990013t.
9
Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: a site-directed spin-labeling study.视紫红质中从螺旋VII延伸至棕榈酰化位点的306 - 322序列的结构特征及光依赖性变化：一项定点自旋标记研究
Biochemistry. 1999 Jun 22;38(25):7931-7. doi: 10.1021/bi9900121.
10
Single-cysteine substitution mutants at amino acid positions 306-321 in rhodopsin, the sequence between the cytoplasmic end of helix VII and the palmitoylation sites: sulfhydryl reactivity and transducin activation reveal a tertiary structure.视紫红质中第306 - 321位氨基酸处的单半胱氨酸取代突变体，即螺旋VII胞质末端与棕榈酰化位点之间的序列：巯基反应性和转导素激活揭示了一种三级结构。
Biochemistry. 1999 Jun 22;38(25):7925-30. doi: 10.1021/bi9900119.

溶液19F核Overhauser效应在哺乳动物视紫红质细胞质结构域结构研究中的应用

Solution 19F nuclear Overhauser effects in structural studies of the cytoplasmic domain of mammalian rhodopsin.

作者信息

Loewen M C, Klein-Seetharaman J, Getmanova E V, Reeves P J, Schwalbe H, Khorana H G

机构信息

Departments of Biology and Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.

出版信息

Proc Natl Acad Sci U S A. 2001 Apr 24;98(9):4888-92. doi: 10.1073/pnas.051633098.

DOI:10.1073/pnas.051633098
PMID:11320239
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC33133/
Abstract

19F nuclear Overhauser effects (NOEs) between fluorine labels on the cytoplasmic domain of rhodopsin solubilized in detergent micelles are reported. Previously, high-resolution solution (19)F NMR spectra of fluorine-labeled rhodopsin in detergent micelles were described, demonstrating the applicability of this technique to studies of tertiary structure in the cytoplasmic domain. To quantitate tertiary contacts we have applied a transient one-dimensional difference NOE solution (19)F NMR experiment to this system, permitting assessment of proximities between fluorine labels specifically incorporated into different regions of the cytoplasmic face. Three dicysteine substitution mutants (Cys-140-Cys-316, Cys-65-Cys-316, and Cys-139-Cys-251) were labeled by attachment of the trifluoroethylthio group through a disulfide linkage. Each mutant rhodopsin was prepared (8-10 mg) in dodecylmaltoside and analyzed at 20 degrees C by solution (19)F NMR. Distinct chemical shifts were observed for all of the rhodopsin (19)F labels in the dark. An up-field shift of the Cys-316 resonance in the Cys-65-Cys-316 mutant suggests a close proximity between the two residues. When analyzed for (19)F-(19)F NOEs, a moderate negative enhancement was observed for the Cys-65-Cys-316 pair and a strong negative enhancement was observed for the Cys-139-Cys-251 pair, indicating proximity between these sites. No NOE enhancement was observed for the Cys-140-Cys-316 pair. These NOE effects demonstrate a solution (19)F NMR method for analysis of tertiary contacts in high molecular weight proteins, including membrane proteins.

摘要

报道了在去污剂胶束中溶解的视紫红质细胞质结构域上氟标签之间的19F核Overhauser效应（NOEs）。此前，已描述了去污剂胶束中氟标记视紫红质的高分辨率溶液（19）F NMR谱，证明了该技术在细胞质结构域三级结构研究中的适用性。为了定量三级接触，我们对该系统应用了瞬态一维差分NOE溶液（19）F NMR实验，从而能够评估特异性掺入细胞质面不同区域的氟标签之间的接近程度。通过二硫键连接三氟乙基硫基，标记了三个双半胱氨酸替代突变体（Cys-140-Cys-316、Cys-65-Cys-316和Cys-139-Cys-251）。每个突变体视紫红质在十二烷基麦芽糖苷中制备（8 - 10毫克），并在20℃下通过溶液（19）F NMR进行分析。在黑暗中，所有视紫红质（19）F标签都观察到了明显的化学位移。Cys-65-Cys-316突变体中Cys-316共振的上移表明这两个残基之间接近。当分析（19）F-（19）F NOEs时，观察到Cys-65-Cys-316对有中等程度的负增强，Cys-139-Cys-251对有强烈的负增强，表明这些位点之间接近。未观察到Cys-140-Cys-316对的NOE增强。这些NOE效应证明了一种用于分析包括膜蛋白在内的高分子量蛋白质三级接触的溶液（19）F NMR方法。