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1
Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: evidence for interaction between ATP and Trp653.多药耐药相关蛋白1核苷酸结合结构域1的生化特性及核磁共振研究：ATP与色氨酸653相互作用的证据
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2
Attempts to characterize the NBD heterodimer of MRP1: transient complex formation involves Gly771 of the ABC signature sequence but does not enhance the intrinsic ATPase activity.对多药耐药相关蛋白1（MRP1）核苷酸结合结构域（NBD）异二聚体进行特性分析的尝试：瞬时复合物形成涉及ABC特征序列的甘氨酸771，但不会增强内在ATP酶活性。
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ATP binding to the first nucleotide-binding domain of multidrug resistance protein MRP1 increases binding and hydrolysis of ATP and trapping of ADP at the second domain.三磷酸腺苷（ATP）与多药耐药蛋白MRP1的第一个核苷酸结合结构域结合，会增加ATP的结合与水解以及二磷酸腺苷（ADP）在第二个结构域的捕获。
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5
Attempts to characterize the NBD heterodimer of MRP1: transient complex formation involves Gly771 of the ABC signature sequence but does not enhance the intrinsic ATPase activity.对多药耐药相关蛋白1（MRP1）核苷酸结合结构域（NBD）异二聚体进行特性分析的尝试：瞬时复合物形成涉及ABC特征序列的甘氨酸771，但不会增强内在ATP酶活性。
Biochem J. 2005 Nov 1;391(Pt 3):481-90. doi: 10.1042/BJ20050897.

本文引用的文献

1
Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1).多药耐药蛋白1（ABCC1）催化循环中与保守核心沃克B基序相邻的羧酸盐残基的作用。
J Biol Chem. 2003 Oct 3;278(40):38537-47. doi: 10.1074/jbc.M305786200. Epub 2003 Jul 27.
2
ATP binding to the first nucleotide binding domain of multidrug resistance-associated protein plays a regulatory role at low nucleotide concentration, whereas ATP hydrolysis at the second plays a dominant role in ATP-dependent leukotriene C4 transport.三磷酸腺苷（ATP）与多药耐药相关蛋白的第一个核苷酸结合结构域结合，在低核苷酸浓度下起调节作用，而在第二个结构域处的ATP水解在ATP依赖的白三烯C4转运中起主导作用。
J Biol Chem. 2003 Aug 15;278(33):30764-71. doi: 10.1074/jbc.M304118200. Epub 2003 Jun 3.
3
ATP binding, not hydrolysis, at the first nucleotide-binding domain of multidrug resistance-associated protein MRP1 enhances ADP.Vi trapping at the second domain.多药耐药相关蛋白MRP1第一个核苷酸结合结构域处的ATP结合而非水解，增强了第二个结构域处ADP.Vi的捕获。
J Biol Chem. 2003 Feb 7;278(6):3599-605. doi: 10.1074/jbc.M210480200. Epub 2002 Nov 27.
4
Nucleotide triphosphatase activity of the N-terminal nucleotide-binding domains of the multidrug resistance proteins P-glycoprotein and MRP1.多药耐药蛋白P-糖蛋白和MRP1的N端核苷酸结合结构域的三磷酸核苷酸酶活性。
Biochem Biophys Res Commun. 2002 Aug 16;296(2):388-94. doi: 10.1016/s0006-291x(02)00878-1.
5
S-decyl-glutathione nonspecifically stimulates the ATPase activity of the nucleotide-binding domains of the human multidrug resistance-associated protein, MRP1 (ABCC1).S-癸基谷胱甘肽非特异性地刺激人多药耐药相关蛋白MRP1（ABCC1）核苷酸结合结构域的ATP酶活性。
Eur J Biochem. 2002 Jul;269(14):3470-8. doi: 10.1046/j.1432-1033.2002.03028.x.
6
The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism.大肠杆菌BtuCD结构：ABC转运蛋白结构与机制的框架
Science. 2002 May 10;296(5570):1091-8. doi: 10.1126/science.1071142.
7
ATP binding to the first nucleotide-binding domain of multidrug resistance protein MRP1 increases binding and hydrolysis of ATP and trapping of ADP at the second domain.三磷酸腺苷（ATP）与多药耐药蛋白MRP1的第一个核苷酸结合结构域结合，会增加ATP的结合与水解以及二磷酸腺苷（ADP）在第二个结构域的捕获。
J Biol Chem. 2002 Feb 15;277(7):5110-9. doi: 10.1074/jbc.M107133200. Epub 2001 Dec 7.
8
Structure of the ABC ATPase domain of human TAP1, the transporter associated with antigen processing.人TAP1（与抗原加工相关的转运体）的ABC ATP酶结构域的结构
EMBO J. 2001 Sep 3;20(17):4964-72. doi: 10.1093/emboj/20.17.4964.
9
Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter.MJ1267 ATP结合盒的晶体结构揭示了ABC转运蛋白ATP酶活性位点处的诱导契合效应。
Structure. 2001 Jul 3;9(7):571-86. doi: 10.1016/s0969-2126(01)00617-7.
10
The human ATP-binding cassette (ABC) transporter superfamily.人类ATP结合盒（ABC）转运蛋白超家族。
Genome Res. 2001 Jul;11(7):1156-66. doi: 10.1101/gr.184901.

多药耐药相关蛋白1核苷酸结合结构域1的生化特性及核磁共振研究：ATP与色氨酸653相互作用的证据

Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: evidence for interaction between ATP and Trp653.

作者信息

Ramaen Odile, Masscheleyn Sandrine, Duffieux Francis, Pamlard Olivier, Oberkampf Marine, Lallemand Jean-Yves, Stoven Véronique, Jacquet Eric

机构信息

Institut de Chimie des Substances Naturelles, Centre National de la Recherche Scientifique (CNRS) Unité Propre de Recherche 2301, Avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, France.

出版信息

Biochem J. 2003 Dec 15;376(Pt 3):749-56. doi: 10.1042/BJ20030998.

DOI:10.1042/BJ20030998
PMID:12954082
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1223803/
Abstract

Multidrug-resistance-associated protein 1 (MRP1/ABCC1) is a human ATP-binding cassette transporter that confers cell resistance to antitumour drugs. Its NBDs (nucleotide-binding domains) bind/hydrolyse ATP, a key step in the activation of MRP1 function. To relate its intrinsic functional features to the mechanism of action of the full-size transporter, we expressed the N-terminal NBD1 domain (Asn(642) to Ser(871)) in Escherichia coli. NBD1 was highly purified under native conditions and was characterized as a soluble monomer. (15)N-labelling allowed recording of the first two-dimensional NMR spectra of this domain. The NMR study showed that NBD1 was folded, and that Trp(653) was a key residue in the NBD1-ATP interaction. Thus, interaction of NBD1 with ATP/ADP was studied by intrinsic tryptophan fluorescence. The affinity for ATP and ADP were in the same range (K (d(ATP))=118 microM and K (d(ADP))=139 microM). Binding of nucleotides did not influence the monomeric state of NBD1. The ATPase activity of NBD1 was magnesium-dependent and very low [V (max) and K (m) values of 5x10(-5) pmol of ATP x (pmol NBD1)(-1) x s(-1) and 833 microM ATP respectively]. The present study suggests that NBD1 has a low contribution to the ATPase activity of full-length MRP1 and/or that this activity requires NBD1-NBD2 heterodimer formation.

摘要

多药耐药相关蛋白1（MRP1/ABCC1）是一种人类ATP结合盒转运蛋白，赋予细胞对抗肿瘤药物的抗性。其核苷酸结合结构域（NBDs）结合/水解ATP，这是MRP1功能激活的关键步骤。为了将其内在功能特征与全长转运蛋白的作用机制联系起来，我们在大肠杆菌中表达了N端的NBD1结构域（天冬酰胺（642）至丝氨酸（871））。NBD1在天然条件下被高度纯化，并被表征为可溶性单体。（15）N标记使得能够记录该结构域的首个二维核磁共振谱。核磁共振研究表明NBD1已折叠，且色氨酸（653）是NBD1与ATP相互作用中的关键残基。因此，通过内在色氨酸荧光研究了NBD1与ATP/ADP的相互作用。对ATP和ADP的亲和力在相同范围内（K（d（ATP））=118微摩尔，K（d（ADP））=139微摩尔）。核苷酸的结合不影响NBD1的单体状态。NBD1的ATP酶活性依赖于镁且非常低[V（max）和K（m）值分别为5×10^（-5）皮摩尔ATP×（皮摩尔NBD1）^（-1）×秒^（-1）和833微摩尔ATP]。本研究表明NBD1对全长MRP1的ATP酶活性贡献较低，和/或该活性需要NBD1 - NBD2异二聚体的形成。