Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin
文献类型：期刊论文
| 作者 | Chang, YG; Song, AX; Gao, YG; Shi, YH; Lin, XJ; Cao, XT; Lin, DH; Hu, HY |
| 刊名 | PROTEIN SCIENCE
 |
| 出版日期 | 2006 |
| 卷号 | 15期号:6页码:1248-1259 |
| 关键词 | ubiquitin-associated domain solution structure complex BMSC-UbP |
| 通讯作者 | Hu, HY (reprint author), Shanghai Inst Biol Sci, Key Lab Proteom, Inst Biochem & Cell Biol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,dhlin@mail.shcnc.ac.cn ; hyhu@sibs.ac.cn |
| 英文摘要 | Ubiquitin is an important cellular signal that targets proteins for degradation or regulates their functions. The previously identified BMSC-UbP protein derived from bone marrow stromal cells contains a ubiquitin-associated(UBA) domain at the C terminus that has been implicated in linking cellular processes and the ubiquitin system. Here, we report the solution NMR structure of the UBA domain of human BMSC-UbP protein and its complex with ubiquitin. The structure determination was facilitated by using a solubility-enhancement tag ( SET) GB1, immunoglobulin G binding domain 1 of Streptococcal protein G. The results show that BMSC-UbP UBA domain is primarily comprised of three alpha-helices with a hydrophobic patch defined by residues within the C terminus of helix-1, loop-1, and helix-3. The M-G-I motif is similar to the M/L-G-F/Y motifs conserved in most UBA domains. Chemical shift perturbation study revealed that the UBA domain binds with the conserved five-stranded beta-sheet of ubiquitin via hydrophobic interactions with the dissociation constant (KD) of similar to 17 mu M. The structural model of BMSC-UbP UBA domain complexed with ubiquitin was constructed by chemical shift mapping combined with the program HADDOCK, which is in agreement with the result from mutagenesis studies. In the complex structure, three residues (Met76, Ile78, and Leu99) of BMSC-UbP UBA form a trident anchoring the domain to the hydrophobic concave surface of ubiquitin defined by residues Leu8, Ile44, His68, and Val70. This complex structure may provide clues for BMSC-UbP functions and structural insights into the UBA domains of other ubiquitin-associated proteins that share high sequence homology with BMSC-UbP UBA domain. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | PROTEIN-PROTEIN INTERACTIONS ; RECEPTOR ENDOCYTOSIS ; BINDING-PROTEIN ; CUE DOMAIN ; PROTEASOME ; NMR ; DOCKING ; PATHWAY ; TSG101 ; RECOGNITION |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000237927900003 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1732]  |
| 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 | Chang, YG,Song, AX,Gao, YG,et al. Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin[J]. PROTEIN SCIENCE,2006,15(6):1248-1259. |
| APA | Chang, YG.,Song, AX.,Gao, YG.,Shi, YH.,Lin, XJ.,...&Hu, HY.(2006).Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin.PROTEIN SCIENCE,15(6),1248-1259. |
| MLA | Chang, YG,et al."Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin".PROTEIN SCIENCE 15.6(2006):1248-1259. |
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