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

• Type: Article in International Scientific Journal
• Date: 1997

Authors

Henriques, EF (Author) Other; Ramos, MJ (Author) FCUP; Reynolds, CA (Author) Other

Journal

Title: Journal of Computer-Aided Molecular Design

Vol. 11

Pages: 547-556

ISSN: 0920-654X

Publisher: Springer Nature

Indexing

ISI Web of Knowledge - 8 Citations

Scopus - 8 Citations

Scientific classification

FOS: Natural sciences > Computer and information sciences

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 10