1.42 angstrom crystal structure of mini-IGF-1(2): an analysis of the disulfide isomerization property and receptor binding property of 1GF-1 based on the three-dimensional structure
文献类型：期刊论文
| 作者 | Yun, CH; Tang, YH; Feng, YM; An, XM; Chang, WR; Liang, DC |
| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2005 |
| 卷号 | 326期号:1页码:52-59 |
| 关键词 | IGF crystal structure disulfide isomerization protein folding receptor binding |
| 通讯作者 | Liang, DC (reprint author), Chinese Acad Sci, Inst Biophys, Natl Key Lab Biomacromol, 15 Datun Rd, Beijing 100101, Chaoyang Dist, Peoples R China.,dcliang@sun5.ibp.ac.cn |
| 英文摘要 | Insulin and insulin-like growth factor 1 (IGF-1) share a homologous sequence, a similar three-dimensional structure and weakly overlapping biological activity, but IGF-1 folds into two thermodynamically stable disulfide isomers, while insulin folds into one unique stable tertiary structure. This is a very interesting phenomenon in which one amino acid sequence encodes two three-dimensional structures, and its molecular mechanism has remained unclear for a long time. In this study, the crystal structure of mini-IGF-1(2), a disulfide isomer of an artificial analog of IGF-1, was solved by the SAD/SIRAS method using our in-house X-ray source. Evidence was found in the structure showing that the intra-A-chain/domain disulfide bond of some molecules was broken; thus, it was proposed that disulfide isomerization begins with the breakdown of this disulfide bond. Furthermore, based on the structural comparison of IGF-1 and insulin, a new assumption was made that in insulin the several hydrogen bonds formed between the N-terminal region of the B-chain and the intra-A-chain disulfide region of the A-chain are the main reason for the stability of the intra-A-chain disulfide bond and for the prevention of disulfide isomerization, while Phe B1 and His B5 are very important for the formation of these hydrogen bonds. Moreover, the receptor binding property of IGF-1 was analyzed in detail based on the structural comparison of mini-IGF-1(2), native IGF-1, and small mini-IGF-1. (C) 2004 Elsevier Inc. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | GROWTH-FACTOR-I ; DIFFERENT FOLDING BEHAVIOR ; INSULIN-RECEPTOR ; B-CHAIN/DOMAIN ; SIDE-CHAIN ; INSULIN-LIKE-GROWTH-FACTOR-1 ; REFINEMENT ; EVOLUTION ; AFFINITY |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000225776600008 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1844]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Yun, CH,Tang, YH,Feng, YM,et al. 1.42 angstrom crystal structure of mini-IGF-1(2): an analysis of the disulfide isomerization property and receptor binding property of 1GF-1 based on the three-dimensional structure[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2005,326(1):52-59. |
| APA | Yun, CH,Tang, YH,Feng, YM,An, XM,Chang, WR,&Liang, DC.(2005).1.42 angstrom crystal structure of mini-IGF-1(2): an analysis of the disulfide isomerization property and receptor binding property of 1GF-1 based on the three-dimensional structure.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,326(1),52-59. |
| MLA | Yun, CH,et al."1.42 angstrom crystal structure of mini-IGF-1(2): an analysis of the disulfide isomerization property and receptor binding property of 1GF-1 based on the three-dimensional structure".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 326.1(2005):52-59. |
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