The dimerization mechanism of the N-terminal domain of spider silk proteins is conserved despite extensive sequence divergence

The N-terminal (NT) domain of spider silk proteins (spidroins) is crucial for their storage at high concentrations and also regulates silk assembly. NTs from the major ampullate spidroin (MaSp) and the minor ampullate spidroin are monomeric at neutral pH and confer solubility to spidroins, whereas a...

Descripción completa

Detalles Bibliográficos
Autores principales: Sarr, Médoune, Kitoka, Kristine, Walsh-White, Kellie-Ann, Kaldmäe, Margit, Metlāns, Rimants, Tārs, Kaspar, Mantese, Alessandro, Shah, Dipen, Landreh, Michael, Rising, Anna, Johansson, Jan, Jaudzems, Kristaps, Kronqvist, Nina
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2022
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9097459/
https://www.ncbi.nlm.nih.gov/pubmed/35398358
http://dx.doi.org/10.1016/j.jbc.2022.101913

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9097459/
https://www.ncbi.nlm.nih.gov/pubmed/35398358
http://dx.doi.org/10.1016/j.jbc.2022.101913

Ejemplares similares