Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity
文献类型：期刊论文
| 作者 | Li, J; Liang, HH ; Wang, L; Wang, CC; Liu, YF; Dong, YH; Niu, YB; Wang, WJ; Dong YH(董宇辉); Wang WJ(王文佳)
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| 刊名 | JOURNAL OF BIOLOGICAL CHEMISTRY
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| 出版日期 | 2018 |
| 卷号 | 293期号:4页码:1192-1202 |
| 关键词 | conformational change molecular chaperone protein structure small-angle X-ray scattering (SAXS) X-ray crystallography |
| ISSN号 | 0021-9258 |
| DOI | 10.1074/jbc.M117.797290 |
| 文献子类 | Article |
| 英文摘要 | Protein-disulfide isomerase-like protein of the testis (PDILT), a member of the protein-disulfide isomerase family, is a chaperone essential for the folding of spermatogenesis-specific proteins in male postmeiotic germ cells. However, the structural mechanisms that regulate the chaperone function of PDILTs are unknown. Here, we report the structures of human PDILT (hPDILT) determined by X-ray crystallography to 2.4 resolution and small-angle X-ray scattering (SAXS). Distinct from previously reported U-like structures of related PDI family proteins, our structures revealed that hPDILT folds into a compact L-like structure in crystals and into an extended chain-like structure in solution. The hydrophobic regions and the hydrophobic pockets in hPDILT, which are important for substrate recognition, were clearly delineated in the crystal structure. Moreover, our results of the SAXS analysis and of structure-based substitutions and truncations indicated that the C-terminal tail in hPDILT is required for suppression of aggregation of denatured proteins, suggesting that the tail is crucial for the chaperone activity of PDILT. Taken together, our findings have identified the critical regions and conformational changes of PDILT that enable and control its activity. These results advance our understanding of the structural mechanisms involved in the chaperone activity of PDILT. |
| 电子版国际标准刊号 | 1083-351X |
| WOS关键词 | SMALL-ANGLE SCATTERING ; REDOX-REGULATED CHAPERONE ; RAY SOLUTION SCATTERING ; MHC CLASS-I ; ENDOPLASMIC-RETICULUM ; BIOLOGICAL MACROMOLECULES ; MISFOLDED PROTEINS ; FOLDING CATALYST ; QUALITY-CONTROL ; BINDING SITE |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000423515000008 |
| 源URL | [http://ir.ihep.ac.cn/handle/311005/285581]  |
| 专题 | 高能物理研究所_多学科研究中心 中国科学院高能物理研究所_中国散裂中子源 |
| 作者单位 | 中国科学院高能物理研究所 |
| 推荐引用方式 GB/T 7714 | Li, J,Liang, HH,Wang, L,et al. Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2018,293(4):1192-1202. |
| APA | Li, J.,Liang, HH.,Wang, L.,Wang, CC.,Liu, YF.,...&Li, HH.(2018).Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity.JOURNAL OF BIOLOGICAL CHEMISTRY,293(4),1192-1202. |
| MLA | Li, J,et al."Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity".JOURNAL OF BIOLOGICAL CHEMISTRY 293.4(2018):1192-1202. |
入库方式： OAI收割
来源：高能物理研究所
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