A molecular dynamics study based post facto free energy analysis of the binding of bovine angiogenin with UMP and CMP ligands.
Indian J Biochem Biophys
;
2001 Feb-Apr; 38(1-2): 27-33
Artigo
em Inglês
| IMSEAR
| ID: sea-27464
ABSTRACT
Angiogenin is a protein belonging to the superfamily of RNase A. The RNase activity of this protein is essential for its angiogenic activity. Although members of the RNase A family carry out RNase activity, they differ markedly in their strength and specificity. In this paper, we address the problem of higher specificity of angiogenin towards cytosine against uracil in the first base binding position. We have carried out extensive nano-second level molecular dynamics(MD) computer simulations on the native bovine angiogenin and on the CMP and UMP complexes of this protein in aqueous medium with explicit molecular solvent. The structures thus generated were subjected to a rigorous free energy component analysis to arrive at a plausible molecular thermodynamic explanation for the substrate specificity of angiogenin.
Texto completo:
DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Assunto principal:
Ligação Proteica
/
Ribonuclease Pancreático
/
Especificidade por Substrato
/
Termodinâmica
/
Uridina Monofosfato
/
Bovinos
/
Modelos Moleculares
/
Monofosfato de Citidina
/
Ligantes
/
Animais
Idioma:
Inglês
Revista:
Indian J Biochem Biophys
Ano de publicação:
2001
Tipo de documento:
Artigo
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