Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant

Raj R.V. Dhanaraj; Jim E. Pitts; Phil Nugent; Ponsook Orprayoon; Jon B. Cooper; Tom L. Blundell; Jaana Uusitalo; Merja Penttila

doi:10.1007/978-1-4615-1871-6_11

Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant

Raj R.V. Dhanaraj^*, Jim E. Pitts, Phil Nugent, Ponsook Orprayoon, Jon B. Cooper, Tom L. Blundell, Jaana Uusitalo, Merja Penttila

^*Corresponding author for this work

University of London: Birkbeck College

Research output: Chapter in Book/Report/Conference proceeding › Conference article in proceedings › Scientific › peer-review

Abstract

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.

Original language	English
Title of host publication	Aspartic Proteinases
Subtitle of host publication	Structure, Function, Biology, and Biomedical Implications
Editors	Kenji Takahashi
Place of Publication	Boston
Publisher	Springer
Pages	95-99
ISBN (Print)	978-1-4613-5761-2
DOIs	https://doi.org/10.1007/978-1-4615-1871-6_11
Publication status	Published - 1 Jan 1995
MoE publication type	A4 Article in a conference publication
Event	5th International Conference on Aspartic Proteinases - Kawashima, Japan Duration: 19 Sept 1993 → 24 Sept 1993 Conference number: 5

Publication series

Series	Advances in Experimental Medicine and Biology
Volume	362
ISSN	0065-2598

Conference

Conference	5th International Conference on Aspartic Proteinases
Country/Territory	Japan
City	Kawashima
Period	19/09/93 → 24/09/93

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10.1007/978-1-4615-1871-6_11

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Dhanaraj, R. R. V., Pitts, J. E., Nugent, P., Orprayoon, P., Cooper, J. B., Blundell, T. L., Uusitalo, J., & Penttila, M. (1995). Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant. In K. Takahashi (Ed.), Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications (pp. 95-99). Springer. https://doi.org/10.1007/978-1-4615-1871-6_11

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title = "Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant",

abstract = "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.",

author = "Dhanaraj, {Raj R.V.} and Pitts, {Jim E.} and Phil Nugent and Ponsook Orprayoon and Cooper, {Jon B.} and Blundell, {Tom L.} and Jaana Uusitalo and Merja Penttila",

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doi = "10.1007/978-1-4615-1871-6_11",

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series = "Advances in Experimental Medicine and Biology",

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Dhanaraj, RRV, Pitts, JE, Nugent, P, Orprayoon, P, Cooper, JB, Blundell, TL, Uusitalo, J & Penttila, M 1995, Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant. in K Takahashi (ed.), Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications. Springer, Boston, Advances in Experimental Medicine and Biology, vol. 362, pp. 95-99, 5th International Conference on Aspartic Proteinases, Kawashima, Japan, 19/09/93. https://doi.org/10.1007/978-1-4615-1871-6_11

Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant. / Dhanaraj, Raj R.V.; Pitts, Jim E.; Nugent, Phil et al.
Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications. ed. / Kenji Takahashi. Boston: Springer, 1995. p. 95-99 (Advances in Experimental Medicine and Biology, Vol. 362).

Research output: Chapter in Book/Report/Conference proceeding › Conference article in proceedings › Scientific › peer-review

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AU - Cooper, Jon B.

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AU - Penttila, Merja

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AB - 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.

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ER -

Dhanaraj RRV, Pitts JE, Nugent P, Orprayoon P, Cooper JB, Blundell TL et al. Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant. In Takahashi K, editor, Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications. Boston: Springer. 1995. p. 95-99. (Advances in Experimental Medicine and Biology, Vol. 362). doi: 10.1007/978-1-4615-1871-6_11

Protein engineering of surface loops: Preliminary X-ray analysis of the CHY155-165RHI mutant

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