3E1R
Midbody targeting of the ESCRT machinery by a non-canonical coiled-coil in CEP55
3E1R の概要
| エントリーDOI | 10.2210/pdb3e1r/pdb |
| 分子名称 | Centrosomal protein of 55 kDa, Programmed cell death 6-interacting protein (3 entities in total) |
| 機能のキーワード | cep55, alix, cytokinesis, escrt, alternative splicing, cell cycle, cell division, coiled coil, mitosis, phosphoprotein, polymorphism, acetylation, apoptosis, cytoplasm, host-virus interaction, protein transport, transport, cell cycle-transport protein complex, cell cycle/transport protein |
| 由来する生物種 | Homo sapiens (Human) 詳細 |
| 細胞内の位置 | Cytoplasm, cytoskeleton, centrosome, centriole: Q53EZ4 Cytoplasm, cytosol: Q8WUM4 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 15118.05 |
| 構造登録者 | Lee, H.H.,Elia, N.,Ghirlando, R.,Lippincott-Schwartz, J.,Hurley, J.H. (登録日: 2008-08-04, 公開日: 2008-11-04, 最終更新日: 2024-02-21) |
| 主引用文献 | Lee, H.H.,Elia, N.,Ghirlando, R.,Lippincott-Schwartz, J.,Hurley, J.H. Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55. Science, 322:576-580, 2008 Cited by PubMed Abstract: The ESCRT (endosomal sorting complex required for transport) machinery is required for the scission of membrane necks in processes including the budding of HIV-1 and cytokinesis. An essential step in cytokinesis is recruitment of the ESCRT-I complex and the ESCRT-associated protein ALIX to the midbody (the structure that tethers two daughter cells) by the protein CEP55. Biochemical experiments show that peptides from ALIX and the ESCRT-I subunit TSG101 compete for binding to the ESCRT and ALIX-binding region (EABR) of CEP55. We solved the crystal structure of EABR bound to an ALIX peptide at a resolution of 2.0 angstroms. The structure shows that EABR forms an aberrant dimeric parallel coiled coil. Bulky and charged residues at the interface of the two central heptad repeats create asymmetry and a single binding site for an ALIX or TSG101 peptide. Both ALIX and ESCRT-I are required for cytokinesis, which suggests that multiple CEP55 dimers are required for function. PubMed: 18948538DOI: 10.1126/science.1162042 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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