Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6JFV

The crystal structure of 2B-2B complex from keratins 5 and 14 (C367A mutant of K14)

Summary for 6JFV
Entry DOI10.2210/pdb6jfv/pdb
DescriptorKeratin, type I cytoskeletal 14, Keratin, type II cytoskeletal 5 (3 entities in total)
Functional Keywordsintermediate filaments, keratinocytes, skin, epithelium, protein self-assembly, cytosolic protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight45061.58
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 citationLee, 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: 31995743
DOI: 10.1016/j.str.2020.01.002
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

226707

数据于2024-10-30公开中

PDB statisticsPDBj update infoContact PDBjnumon