Utilize este identificador para referenciar este registo: http://hdl.handle.net/10362/179535
Título: Unveiling the structural basis of the complex between the virulence factor SARS-CoV2 Nsp1 and the host DNA polymerase-alpha
Outros títulos: A step forward for the development of new antiviral drugs
Autor: Salgueiro, Bruno
Orientador: Romão, Célia
Moe, Elin
Matias, Pedro
Palavras-chave: Coronavirus
Non-structural protein 1
RNA/DNA nuclease activity
divalent metals
proteolytic activity
Data de Defesa: 19-Dez-2024
Resumo: "The work presented in this dissertation focuses on studies of the Non-structural protein 1 (Nsp1) of SARS-CoV2 (Nsp1SARS-CoV2), identified as a major virulence factor causing Covid 19. Nsp1 is a small protein encoded by ORF1a/b and is found only in the a/b- Coronavirus (a/b-CoV) genera. SARS-CoV2 belongs to the b-CoV, and Nsp1 proteins from these genera consist of two structural domains: a globular N-terminal domain (NTD) and a flexible Cterminal domain (CTD), connected to the NTD by a loop (L) of approximately 28 amino acids. Despite the low sequence identity across Nsp1 proteins, they all share the same structural fold for the NTD.(...)"
URI: http://hdl.handle.net/10362/179535
Designação: Dissertation presented to obtain the PhD degree in Molecular Biosciences
Aparece nas colecções:ITQB: SG - PhD Theses

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