6JLB
Crystal structure of lamin A/C fragment and assembly mechanisms of intermediate filaments
6JLB の概要
| エントリーDOI | 10.2210/pdb6jlb/pdb |
| 分子名称 | Lamin A/C (1 entity in total) |
| 機能のキーワード | nuclear lamin, coiled-coil structure, intermediate filaments, 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 | 140222.52 |
| 構造登録者 | |
| 主引用文献 | Ahn, J.,Jo, I.,Kang, S.M.,Hong, S.,Kim, S.,Jeong, S.,Kim, Y.H.,Park, B.J.,Ha, N.C. Structural basis for lamin assembly at the molecular level. Nat Commun, 10:3757-3757, 2019 Cited by PubMed Abstract: Nuclear structure and function are governed by lamins, which are intermediate filaments that mostly consist of α-helices. Different lamin assembly models have been proposed based on low resolution and fragmented structures. However, their assembly mechanisms are still poorly understood at the molecular level. Here, we present the crystal structure of a long human lamin fragment at 3.2 Å resolution that allows the visualization of the features of the full-length protein. The structure shows an anti-parallel arrangement of the two coiled-coil dimers, which is important for the assembly process. We further discover an interaction between the lamin dimers by using chemical cross-linking and mass spectrometry analysis. Based on these two interactions, we propose a molecular mechanism for lamin assembly that is in agreement with a recent model representing the native state and could explain pathological mutations. Our findings also provide the molecular basis for assembly mechanisms of other intermediate filaments. PubMed: 31434876DOI: 10.1038/s41467-019-11684-x 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.205 Å) |
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