6JFV
The crystal structure of 2B-2B complex from keratins 5 and 14 (C367A mutant of K14)
Summary for 6JFV
Entry DOI | 10.2210/pdb6jfv/pdb |
Descriptor | Keratin, type I cytoskeletal 14, Keratin, type II cytoskeletal 5 (3 entities in total) |
Functional Keywords | intermediate filaments, keratinocytes, skin, epithelium, protein self-assembly, cytosolic protein |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 4 |
Total formula weight | 45061.58 |
Authors | Kim, M.S.,Lee, C.H.,Coulombe, P.A.,Leahy, D.J. (deposition date: 2019-02-12, release date: 2020-01-22, Last modification date: 2024-05-29) |
Primary citation | Lee, C.H.,Kim, M.S.,Li, S.,Leahy, D.J.,Coulombe, P.A. Structure-Function Analyses of a Keratin Heterotypic Complex Identify Specific Keratin Regions Involved in Intermediate Filament Assembly. Structure, 28:355-362.e4, 2020 Cited by PubMed Abstract: Intermediate filaments (IFs) provide vital mechanical support in a broad array of cell types. Interference with this role causes cell fragility and accounts for a large number of human diseases. Gaining an understanding of the structure of IFs is paramount to understanding their function and designing therapeutic agents for relevant diseases. Here, we report the 2.6-Å resolution crystal structure of a complex of interacting 2B domains of keratin 5 (K5) and K14. K5 and K14 form a long-range, left-handed coiled coil, with participating α helices aligned in parallel and in register. Follow-up mutagenesis revealed that specific contacts between interacting 2B domains play a crucial role during 10-nm IF assembly, likely at the step of octamer-octamer association. The resulting structural model represents an atomic-resolution visualization of 2B-2B interactions important to filament assembly and provides insight into the defects introduced by mutations in IF genes associated with human skin diseases. PubMed: 31995743DOI: 10.1016/j.str.2020.01.002 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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