Inclusion of conserved buried water molecules in the model structure of rat submaxillary kallikrein

• Tipo: Artigo em Revista Científica Internacional
• Data: 1997

Autores

Henriques, EF (Autor) Outra; Ramos, MJ (Autor) FCUP; Reynolds, CA (Autor) Outra

Revista

Título: Journal of Computer-Aided Molecular Design

Vol. 11

Páginas: 547-556

ISSN: 0920-654X

Editora: Springer Nature

Indexação

ISI Web of Knowledge - 8 Citações

Scopus - 8 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências da computação e da informação

Outras Informações

ID Authenticus: P-001-ACH

DOI: 10.1023/a:1007919812771

Abstract (EN): A new approach to the molecular modelling of homologous serine proteases is adopted, by including a set of 21 buried waters known to be preserved in enzymes sharing the primary specificity of trypsin, in the homology modelling of rat submaxillary gland kallikrein. Buried waters - water molecules sequestered from bulk solvent within a protein matrix - appear to be integral conserved components of all serine proteases of known structure and should be incorporated into serine protease models built on the basis of sequence/structural homology to this family. The absence of such waters might induce errors in a force field simulation, favouring the formation of nonexistent hydrogen bonds and locally inaccurate structure. The kallikrein model refinement has led to the conclusion that an additional buried water should be added to the original rigid matrix of 21 conserved water molecules. The structurally preserved protein cavities of such waters validate the modelled structure.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 10