3KLT
Crystal structure of a vimentin fragment
3KLT の概要
| エントリーDOI | 10.2210/pdb3klt/pdb |
| 分子名称 | Vimentin, 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL, SAMARIUM (III) ION, ... (9 entities in total) |
| 機能のキーワード | 2a, l2, alpha-helix, coiled-coil, parallel helices, coiled coil, intermediate filament, vimentin, structural protein |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 35281.50 |
| 構造登録者 | |
| 主引用文献 | Nicolet, S.,Herrmann, H.,Aebi, U.,Strelkov, S.V. Atomic structure of vimentin coil 2. J.Struct.Biol., 170:369-376, 2010 Cited by PubMed Abstract: Intermediate filaments (IFs) are essential cytoskeletal components in metazoan cells. They assemble from elementary dimers that are built around the central alpha-helical coiled-coil rod domain representing the IF 'signature'. The rod consists of two similarly-sized parts, coil 1 and coil 2, connected by a non-alpha-helical linker L12. Coil 2 is absolutely conserved in length across all IF types and was initially predicted to consist of a short coiled-coil segment 2A based on a heptad pattern of hydrophobic residues, another linker L2 and a coiled-coil segment 2B. Here we present the crystal structure of human vimentin fragment including residues 261-335 i.e. approximately the first half of coil 2. The N-terminal part of this fragment reveals a parallel alpha-helical bundle characterized by 3.5 consecutive hendecad repeats. It is immediately followed by a regular left-handed coiled coil. The distinct non-helical linker L2 is therefore not observed. Together with the previously determined crystal structure of the major part of segment 2B (Strelkov et al., 2002), we can now build a complete atomic model of the 21nm long vimentin coil 2 dimer being a relatively rigid rod. PubMed: 20176112DOI: 10.1016/j.jsb.2010.02.012 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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