1H, 15N, and 13C resonance assignments of the SH3-like tandem domain of human KIN protein

• Autor(a) principal: de Lourenço, Isabella Otenio [UNESP]
• Data de Publicação: 2021
• Outros Autores: Seixas, Flávio Augusto Vicente, Fernandez, Maria Aparecida, Almeida, Fabio Ceneviva Lacerda, Fossey, Marcelo Andrés [UNESP], de Souza, Fátima Pereira [UNESP], Caruso, Ícaro Putinhon [UNESP]
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNESP
• Texto Completo: http://dx.doi.org/10.1007/s12104-021-10044-5; http://hdl.handle.net/11449/229372
• topic: Human KIN protein; NMR assignment; SH3-like tandem domain

KIN is a DNA/RNA-binding protein conserved evolutionarily from yeast to humans and expressed ubiquitously in mammals. It is an essential nuclear protein involved in numerous cellular processes, such as DNA replication, class-switch recombination, cell cycle regulation, and response to UV or ionizing radiation-induced DNA damage. The C-terminal region of the human KIN (hKIN) protein is composed of an SH3-like tandem domain, which is crucial for the anti-proliferation effect of the full-length protein. Herein, we present the 1H, 15N, and 13C resonances assignment of the backbone and side chains for the SH3-like tandem domain of the hKIN protein, as well as the secondary structure prediction based on the assigned chemical shifts using TALOS-N software. This work prepares the ground for future studies of RNA-binding and backbone dynamics.