6jfv
From Proteopedia
The crystal structure of 2B-2B complex from keratins 5 and 14 (C367A mutant of K14)
Structural highlights
Disease[K1C14_HUMAN] Epidermolysis bullosa simplex, Dowling-Meara type;Localized epidermolysis bullosa simplex;Dermatopathia pigmentosa reticularis;Naegeli-Franceschetti-Jadassohn syndrome;Epidermolysis bullosa simplex with mottled pigmentation;Generalized epidermolysis bullosa simplex, non-Dowling-Meara type;KRT14-related epidermolysis bullosa simplex. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. [K2C5_HUMAN] Epidermolysis bullosa simplex, Dowling-Meara type;Localized epidermolysis bullosa simplex;Epidermolysis bullosa simplex with circinate migratory erythema;Epidermolysis bullosa simplex with mottled pigmentation;Dowling-Degos disease;Generalized epidermolysis bullosa simplex, non-Dowling-Meara type. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function[K1C14_HUMAN] The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro.[1] Publication Abstract from PubMedIntermediate 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-A 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 alpha 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. Structure-Function Analyses of a Keratin Heterotypic Complex Identify Specific Keratin Regions Involved in Intermediate Filament Assembly.,Lee CH, Kim MS, Li S, Leahy DJ, Coulombe PA Structure. 2020 Mar 3;28(3):355-362.e4. doi: 10.1016/j.str.2020.01.002. Epub 2020, Jan 28. PMID:31995743[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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