Protein Engineering of Surface Loops: Preliminary X-Ray Analysis of the Chy155–165rhi Mutant

Autor: Merja Penttilä, Raj R. V. Dhanaraj, Jon B. Cooper, Janna Uusitalo, Poonsook Orprayoon, Phil Nugent, J. E. Pitts, Tom L. Blundell
Rok vydání: 1995
Předmět:
Zdroj: Aspartic Proteinases ISBN: 9781461357612
DOI: 10.1007/978-1-4615-1871-6_11
Popis: The protein engineering programme at Birkbeck seeks to develop generic methods based on a design cycle involving biochemical preparation and characterization, determination and comparative analysis of three-dimensional structures, rule-based design, site-directed mutagenesis and expression of the mutants. Knowledge of the tertiary structure of proteins and the use of molecular modelling techniques provide a powerful approach for the design of novel biomolecules with specifically engineered properties. The aspartic proteinase family have been studied in detail by X-ray analysis and provide a suitable data base for the development of protein engineering design principles1–6. This family of endopeptidases belonging to a wide range of biological species with varying substrate specificities. The members of the family are of considerable commercial importance since enzymes such as chymosin and Mucor pusillus pepsin have been exploited by the food industry in cheese and soya processing, while renins, cathepsins and the retroviral proteinases are prime targets of the pharmaceutical industries in drug design.
Databáze: OpenAIRE