Mutagenesis of the three conserved valine residues: consequence on the foldability of insulin
文献类型：期刊论文
| 作者 | Guo, ZY; Wang, S; Tang, YH; Feng, YM |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
 |
| 出版日期 | 2004 |
| 卷号 | 1699期号:1页码:103-109 |
| 关键词 | insulin foldability secretion refolding stability |
| 通讯作者 | Feng, YM (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Key Lab Proteom, Inst Biochem & Cell Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,fengym@sunm.shcnc.ac.cn |
| 英文摘要 | Natural polypeptide chain usually can spontaneously fold into tightly compact native structure. This capability is the so-called foldability. However, how the foldability is encoded in the polypeptide chain is still poorly understood. The structure of insulin has been well solved and extensively investigated. Therefore, insulin provides a good model for investigating the role of individual residue to the sequence foldability. In insulins from different species there are three highly conserved Val residues (A3Val, B12Val, and B18Val), but their contribution to the insulin foldability is still unknown. Here, a single-chain insulin (PIP) was used to investigate the contribution of the three conserved valine residues to the foldability. Five PIP mutants, [A3S]PIP, [A3T]PIP, [B12A]PIP, [B18T]PIP, and [B18L]PIP, were used in the studies, and their structural changes, secretion efficiency, structural stability, disulfide stability, and in vitro refolding efficiency were analyzed. The effects of the mutations on the PIP foldability are multifold: as a whole, mutation of A3Val has only moderate effect; while mutation of B12Val has significant detriment; hydrophobic replacement of B18Val is more tolerant than hydrophilic substitution as foldability is concerned. Therefore, the three highly conserved valine residues have different contributions to the insulin foldability, and their contribution might be ranked as B12Val>B18Val>A3Val. (C) 2004 Elsevier B.V. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | RECEPTOR-BINDING ; MUTATIONAL ANALYSIS ; MOLECULE ; MONOMER ; PATHWAY ; SURFACE ; DESIGN ; CHAINS ; ANALOG |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000221807800009 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2195]  |
| 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 | Guo, ZY,Wang, S,Tang, YH,et al. Mutagenesis of the three conserved valine residues: consequence on the foldability of insulin[J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,2004,1699(1):103-109. |
| APA | Guo, ZY,Wang, S,Tang, YH,&Feng, YM.(2004).Mutagenesis of the three conserved valine residues: consequence on the foldability of insulin.BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS,1699(1),103-109. |
| MLA | Guo, ZY,et al."Mutagenesis of the three conserved valine residues: consequence on the foldability of insulin".BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS 1699.1(2004):103-109. |
入库方式： OAI收割
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。