NMR SOLUTION STRUCTURE OF AN ALPHA-BUNGAROTOXIN NICOTINIC RECEPTOR PEPTIDE COMPLEX
文献类型：期刊论文
| 作者 | BASUS, VJ; SONG, GQ; HAWROT, E |
| 刊名 | BIOCHEMISTRY
 |
| 出版日期 | 1993-11-23 |
| 卷号 | 32期号:46页码:12290-12298 |
| ISSN号 | 0006-2960 |
| DOI | 10.1021/bi00097a004 |
| 文献子类 | Article |
| 英文摘要 | We report the two-dimensional nuclear magnetic resonance (NMR) characterization of the stoichiometric complex formed between the snake venom-derived long alpha-neurotoxin, alpha-bungarotoxin (BGTX), and a synthetic dodecapeptide (alpha185-196) corresponding to a functionally important region on the alpha-subunit of the nicotinic acetylcholine receptor (nAChR) obtained from Torpedo californica electric organ tissue. BGTX has been widely used as the classic nicotinic competitive antagonist for the skeletal muscle type of nAChR which is found in the avian, amphibian, and mammalian neuromuscular junction. The receptor dodecapeptide (alpha185-196) binds BGTX with micromolar affinity and has been shown to represent the major determinant of BGTX binding to the isolated alpha-subunit. Previous studies involving covalent modification of the native nAChR from Torpedo membranes with a variety of affinity reagents indicate that several residues contained within the dodecapeptide sequence (namely, Tyr-190, Cys-192, and Cys-193) apparently contribute directly to the formation of the cholinergic ligand binding site. The NMR-derived solution structure of the BGTX/receptor peptide complex defines a relatively extended conformation for a major segment of the ''bound'' dodecapeptide. These structural studies also reveal a previously unpredicted receptor binding cleft within BGTX and suggest that BGTX undergoes a conformational change upon peptide binding. If, as we hypothesize, the identified intermolecular contacts in the BGTX/receptor peptide complex describe a portion of the contact zone between BGTX and native receptor, then the structural data would suggest that alpha-subunit residues 186-190 are on the extracellular surface of the receptor. |
| WOS关键词 | TORPEDO ACETYLCHOLINE-RECEPTOR ; NUCLEAR-MAGNETIC-RESONANCE ; SITE-DIRECTED MUTAGENESIS ; NAJA-NIGRICOLLIS VENOM ; BINDING-SITE ; CRYSTAL-STRUCTURE ; SECONDARY STRUCTURE ; AMINO-ACIDS ; INTRINSIC FLUORESCENCE ; SYNTHETIC PEPTIDES |
| 资助项目 | NIGMS NIH HHS[GM32629] ; NCRR NIH HHS[RR01695] |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:A1993MH74600004 |
| 出版者 | AMER CHEMICAL SOC |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/275115]  |
| 专题 | 中国科学院上海药物研究所 |
| 作者单位 | 1.ACAD SINICA, SHANGHAI INST MATERIA MED, SHANGHAI 200031, PEOPLES R CHINA 2.BROWN UNIV, DIV BIOL & MED, MOLEC & BIOCHEM PHARMACOL SECT, PROVIDENCE, RI 02912 USA 3.UNIV CALIF SAN FRANCISCO, DEPT PHARMACEUT CHEM, SAN FRANCISCO, CA 94143 USA |
| 推荐引用方式 GB/T 7714 | BASUS, VJ,SONG, GQ,HAWROT, E. NMR SOLUTION STRUCTURE OF AN ALPHA-BUNGAROTOXIN NICOTINIC RECEPTOR PEPTIDE COMPLEX[J]. BIOCHEMISTRY,1993,32(46):12290-12298. |
| APA | BASUS, VJ,SONG, GQ,&HAWROT, E.(1993).NMR SOLUTION STRUCTURE OF AN ALPHA-BUNGAROTOXIN NICOTINIC RECEPTOR PEPTIDE COMPLEX.BIOCHEMISTRY,32(46),12290-12298. |
| MLA | BASUS, VJ,et al."NMR SOLUTION STRUCTURE OF AN ALPHA-BUNGAROTOXIN NICOTINIC RECEPTOR PEPTIDE COMPLEX".BIOCHEMISTRY 32.46(1993):12290-12298. |
入库方式： OAI收割
来源：上海药物研究所
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