Length of central α-helical coiled-coil rod domain that lamin monomer is composed of

Range ~50 nm
Organism Chicken Gallus gallus
Reference Turgay Y et al., (2017). The molecular architecture of lamins in somatic cells. Nature. 2017 Mar 9 543(7644):261-264. doi: 10.1038/nature21382 p.263 right column 3rd paragraphPubMed ID28241138
Primary Source [18] Heitlinger, E. et al. Expression of chicken lamin B2 in Escherichia coli: characterization of its structure, assembly, and molecular interactions. J. Cell Biol. 113, 485–495 (1991)PubMed ID2016332
Method Abstract: "Here [investigators] use cryo-electron tomography to obtain a detailed view of the organization of the lamin meshwork within the lamina. Data analysis of individual lamin filaments resolves a globular-decorated fibre appearance and shows that A- and B-type lamins assemble into tetrameric filaments of 3.5nm thickness."
Comments P.263 right column 3rd paragraph: "Lamin monomers are composed of a central α-helical coiled-coil rod domain, ~50 nm in length [primary source], flanked by a non-α-helical amino (N)-terminal head and a carboxy (C)-terminal tail domain [ref 19]. The head domain is short (~ 30 amino acids) [ref 20], while the tail domain is 185–277 residues long and includes a globular immunoglobulin-fold, ~3.5 nm in diameter [ref 21]. In solution, lamins form parallel and in register dimers exhibiting two immunoglobulin-fold domains located within the C-terminal end of the rod. The dimers further assemble into head-to-tail polymers, arranged in a partly staggered conformation, in which immunoglobulin domains are found distributed at ~40 nm intervals (Extended Data Fig. 5c), causing the characteristic beaded appearance of lamin assemblies [refs 17,22]."
Entered by Uri M
ID 114287