Structural study on two tandem helix bundles of the rod domain of talin, an integrin activator
文献类型：期刊论文
| 作者 | Lin Lin1,2; Song Xian-Qiang1; Ye Sheng1; Zhang Rong-Guang1 |
| 刊名 | Progress in biochemistry and biophysics
 |
| 出版日期 | 2015-06-01 |
| 卷号 | 42期号:6页码:574-582 |
| 关键词 | Talin R9-10 R10-11 Crystal structure Tandem helix bundles Auto-inhibition |
| ISSN号 | 1000-3282 |
| 通讯作者 | Zhang rong-guang(rzhang@ibp.ac.cn) |
| 英文摘要 | Talin, as the activator of integrin and the adaptor between the cytoskeleton and integrin, plays a key role in a series of processes such as cell adhesion and migration. the activation of integrin involves f3 subdomain of talin-ferm domain binding the cytoplasmic tail of integrin beta-subunit. talin has two states: auto-inhibited and activated. we previously reported the auto-inhibition complex structure of talin f2f3/r9, in which the integrin binding site f3 interacts with r9(1654 similar to 1822 a.a.) of talin-rod, such that integrin cannot be activated. however, besides f3 and r9, it remains unclear what structural or functional roles the other domains of the 270 ku talin play in the regulation of its activation. here we solved the crystal structures of talin r9-r10 (1654 similar to 1973 a.a.) and r10-r11 (1815 similar to 2140 a.a.), respectively. r9, r10 and r11 are all 5-helix bundles. r9 and r10 is joined together by a long alpha-helix instead of a flexible loop, and the two bundles are located at the opposite sides of the long helix with an angle of about 150 degrees. the linker between r10 and r11 is stabilized by neighboring hydrogen bonds, forming an angle of about 120 between the two bundles. these angles observed in our crystal structures are consistent with the previously reported saxs and em results. after superimposition of r9-10, r10-11 with previously reported structures of r7-8 and r11-12, a model of r7-12 was acquired, which adopts an elongated linear conformation, except that r8 protrudes from the rod. according to this model, r10-12 does not intrude the interaction between f3 and r9, whereas r8 not only masks the f3 binding site of r9, but also might electrostatically hinders f2f3 approaching via its unique positively charged surface. this hypothesis was further verified by the results of size exclusion chromatography. our work provides a new structural basis for studying the mechanism of talin auto-inhibition. |
| WOS关键词 | VINCULIN-BINDING ; CELL-ADHESION ; PROTEIN ; DISRUPTION ; MECHANISM ; TAILS ; ACTIN ; HEAD |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| WOS类目 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:000356911300010 |
| 出版者 | CHINESE ACAD SCIENCES, INST BIOPHYSICS |
| URI标识 | http://www.irgrid.ac.cn/handle/1471x/2376387 |
| 专题 | 中国科学院大学 |
| 通讯作者 | Zhang Rong-Guang |
| 作者单位 | 1.Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Lin Lin,Song Xian-Qiang,Ye Sheng,et al. Structural study on two tandem helix bundles of the rod domain of talin, an integrin activator[J]. Progress in biochemistry and biophysics,2015,42(6):574-582. |
| APA | Lin Lin,Song Xian-Qiang,Ye Sheng,&Zhang Rong-Guang.(2015).Structural study on two tandem helix bundles of the rod domain of talin, an integrin activator.Progress in biochemistry and biophysics,42(6),574-582. |
| MLA | Lin Lin,et al."Structural study on two tandem helix bundles of the rod domain of talin, an integrin activator".Progress in biochemistry and biophysics 42.6(2015):574-582. |
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来源：中国科学院大学
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