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1
Specificity of interactions of hapten side chains with the combining site of the myeloma protein MOPC 315.半抗原侧链与骨髓瘤蛋白MOPC 315结合位点相互作用的特异性
Biochem J. 1977 Aug 1;165(2):227-35. doi: 10.1042/bj1650227.
2
The combining site of the dinitrophenyl-binding immunoglobulin A myeloma protein MOPC 315.二硝基苯基结合免疫球蛋白A骨髓瘤蛋白MOPC 315的结合位点。
Biochem J. 1977 Aug 1;165(2):207-23. doi: 10.1042/bj1650207.
3
The gross architecture of an antibody-combining site as determined by spin-label mapping.通过自旋标记图谱测定的抗体结合位点的总体结构。
Biochem J. 1977 Aug 1;165(2):177-97. doi: 10.1042/bj1650177.
4
Antibody--hapten interactions in solution.溶液中的抗体 - 半抗原相互作用。
Philos Trans R Soc Lond B Biol Sci. 1975 Nov 6;272(915):53-74. doi: 10.1098/rstb.1975.0070.
5
Comparison of the dimensions of the combining sites of the dinitrophenyl-binding immunoglobulin A myeloma proteins MOPC 315, MOPC 460 and XRPC 25 by spin-label mapping.通过自旋标记图谱比较二硝基苯基结合免疫球蛋白A骨髓瘤蛋白MOPC 315、MOPC 460和XRPC 25结合位点的尺寸。
Biochem J. 1977 Aug 1;165(2):199-206. doi: 10.1042/bj1650199.
6
Resonance Raman-spectroscopic studies of the hapten features involved in the binding of 2,4-dinitrophenyl haptens by the mouse myeloma proteins MOPC 315 and MOPC 460.对小鼠骨髓瘤蛋白MOPC 315和MOPC 460与2,4-二硝基苯基半抗原结合所涉及的半抗原特征进行共振拉曼光谱研究。
Biochem J. 1978 Nov 1;175(2):727-35. doi: 10.1042/bj1750727.
7
The binding of 2,4,6-trinitrophenyl derivatives to the mouse myeloma immunoglobulin A protein MOPC 315.2,4,6-三硝基苯基衍生物与小鼠骨髓瘤免疫球蛋白A蛋白MOPC 315的结合
Biochem J. 1978 Jan 1;169(1):179-88. doi: 10.1042/bj1690179.
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Structure of an antibody combining site by magnetic resonance.通过磁共振解析抗体结合位点的结构。
Nature. 1977 Mar 3;266(5597):31-7. doi: 10.1038/266031a0.
9
Interactions of the lanthanide- and hapten-binding sites in the Fv fragment from the myeloma protein MOPC 315.骨髓瘤蛋白MOPC 315的Fv片段中镧系元素结合位点与半抗原结合位点的相互作用。
Biochem J. 1976 Apr 1;155(1):37-53. doi: 10.1042/bj1550037.
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Circular dichroism of hapten--antibody complexes: characterization of the combining sites of native and reformed MOPC-315 protein, its isolated subunits, and its Fv fragment.半抗原-抗体复合物的圆二色性：天然及改造后的MOPC-315蛋白、其分离亚基及其Fv片段结合位点的表征
Scand J Immunol. 1976;5(6-7):655-66. doi: 10.1111/j.1365-3083.1976.tb03015.x.

引用本文的文献

1
The variability of nitro group--protein interaction in the 2,4-dinitrophenyl-binding antibodies M315, M460 and X25 investigated by resonance Raman spectroscopy.通过共振拉曼光谱研究的2,4-二硝基苯基结合抗体M315、M460和X25中硝基与蛋白质相互作用的变异性。
Biochem J. 1981 Jul 1;197(1):119-25. doi: 10.1042/bj1970119.
2
The combining site of the dinitrophenyl-binding immunoglobulin A myeloma protein MOPC 315.二硝基苯基结合免疫球蛋白A骨髓瘤蛋白MOPC 315的结合位点。
Biochem J. 1977 Aug 1;165(2):207-23. doi: 10.1042/bj1650207.
3
The binding of 2,4,6-trinitrophenyl derivatives to the mouse myeloma immunoglobulin A protein MOPC 315.2,4,6-三硝基苯基衍生物与小鼠骨髓瘤免疫球蛋白A蛋白MOPC 315的结合
Biochem J. 1978 Jan 1;169(1):179-88. doi: 10.1042/bj1690179.
4
The gross architecture of an antibody-combining site as determined by spin-label mapping.通过自旋标记图谱测定的抗体结合位点的总体结构。
Biochem J. 1977 Aug 1;165(2):177-97. doi: 10.1042/bj1650177.

本文引用的文献

1
A high resolution structure of an inhibitor complex of the extracellular nuclease of Staphylococcus aureus. I. Experimental procedures and chain tracing.金黄色葡萄球菌细胞外核酸酶抑制剂复合物的高分辨率结构。I. 实验步骤和链追踪
J Biol Chem. 1971 Apr 10;246(7):2302-16.
2
An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity.本斯·琼斯蛋白和骨髓瘤轻链可变区序列分析及其对抗体互补性的影响。
J Exp Med. 1970 Aug 1;132(2):211-50. doi: 10.1084/jem.132.2.211.
3
Attempts to locate complementarity-determining residues in the variable positions of light and heavy chains.尝试在轻链和重链可变区定位互补决定残基。
Ann N Y Acad Sci. 1971 Dec 31;190:382-93. doi: 10.1111/j.1749-6632.1971.tb13550.x.
4
Affinity labeling and cross-linking of the heavy and light chains of a myeloma protein with anti-2,4-dinitrophenyl activity.具有抗2,4 - 二硝基苯基活性的骨髓瘤蛋白重链和轻链的亲和标记及交联
Biochemistry. 1971 Aug 31;10(18):3461-6. doi: 10.1021/bi00794a023.
5
Localization of affinity-labeled residues on the heavy and light chain of two myeloma proteins with anti-hapten activity.具有抗半抗原活性的两种骨髓瘤蛋白重链和轻链上亲和标记残基的定位
Biochemistry. 1972 Jun 20;11(13):2389-98. doi: 10.1021/bi00763a001.
6
Mathematical models for interacting groups in nuclear magnetic resonance titration curves.核磁共振滴定曲线中相互作用基团的数学模型。
Biochemistry. 1972 Feb 15;11(4):541-7. doi: 10.1021/bi00754a010.
7
Affinity labeling of a mouse myeloma protein which binds nitrophenyl ligands. Sequence and position of a labeled tryptic peptide.一种结合硝基苯基配体的小鼠骨髓瘤蛋白的亲和标记。标记的胰蛋白酶肽段的序列和位置。
Biochemistry. 1970 Sep 29;9(20):3862-71. doi: 10.1021/bi00822a003.
8
Kinetic mapping of the antibody combining site by chemical relaxation spectrometry.通过化学弛豫光谱法对抗体结合位点进行动力学图谱分析。
Biochemistry. 1974 May 7;13(10):2210-22. doi: 10.1021/bi00707a030.
9
Amino acid sequence of the light chain of a mouse myeloma protein (MOPC-315).一种小鼠骨髓瘤蛋白（MOPC - 315）轻链的氨基酸序列。
Biochemistry. 1973 Dec 18;12(26):5400-16.
10
Localization of antibody-combining sites within the variable portions of heavy and light chains.抗体结合位点在重链和轻链可变区的定位。
Proc Natl Acad Sci U S A. 1972 Sep;69(9):2659-62. doi: 10.1073/pnas.69.9.2659.

半抗原侧链与骨髓瘤蛋白MOPC 315结合位点相互作用的特异性

Specificity of interactions of hapten side chains with the combining site of the myeloma protein MOPC 315.

作者信息

Wain-Hobson S, Dower S K, Gettins P, Givol D, McLaughlin A C, Pecht I, Sunderland C A, Dwek R A

出版信息

Biochem J. 1977 Aug 1;165(2):227-35. doi: 10.1042/bj1650227.

DOI:10.1042/bj1650227
PMID:921746
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1164893/
Abstract

The pKa values of the three histidine residues in the Fv fragment (variable region of the heavy and light chains) of the mouse myeloma protein MOPC 315, measured by high resolution n.m.r. (nuclear magnetic resonance), are 5.9, 6.9 and 8.2. The perturbation of the pKa of one of the histidines (pKa 6.9) on the addition of hapten and the narrow linewidth of its proton resonances suggests that it is at the edge of the combining site. References to the model of the Fv fragment [Padlan, Davies, Pecht, Givol & Wright (1976) Cold Spring Harbor Symp. Quant. Biol. 41, in the press] allows assignment of the three histidine residues, histidine-102H, histidine-97L and histidine-44L. The determination of the pKa of the phosphorus group, by 31P n.m.r., of a homologous series of Dnp- and Tnp- (di- and tri-nitrophenyl) haptens has located a positively charged residue. Molecular-model studies on the conformations of these haptens show that the residue is at the edge of the site. The model suggests that the positively charged residue is either arginine-95L or lysine-52H.

摘要

通过高分辨率核磁共振（n.m.r.）测得的小鼠骨髓瘤蛋白MOPC 315的Fv片段（重链和轻链可变区）中三个组氨酸残基的pKa值分别为5.9、6.9和8.2。添加半抗原时其中一个组氨酸（pKa 6.9）的pKa受到扰动，且其质子共振线宽较窄，这表明它位于结合位点的边缘。参考Fv片段模型[帕德兰、戴维斯、佩希特、吉沃尔和赖特（1976年）《冷泉港定量生物学研讨会》第41卷，即将出版]可确定这三个组氨酸残基分别为组氨酸-102H、组氨酸-97L和组氨酸-44L。通过31P n.m.r.对一系列同源的二硝基苯（Dnp）和三硝基苯（Tnp）半抗原的磷基团pKa进行测定，确定了一个带正电荷的残基。对这些半抗原构象的分子模型研究表明，该残基位于位点的边缘。该模型表明，带正电荷的残基要么是精氨酸-95L，要么是赖氨酸-52H。