Contact information
David Stammers
Professor of Structural Biology
A major research interest of the Group relates to the structural biology of potential target enzymes for development of anti-microbial drugs and understanding the basis for mutations giving rise to drug resistance. A second topic concerns structure determination of some regulatory proteins involved in transcription and membrane transport. The techniques we use range from cloning, expression and purification of proteins for crystallisation and structure determination by X-ray crystallography. We have determined structures of essential gene products as potential novel targets for the development of antibacterial drugs (e.g. YeaZ, YegS, riba, AKIII). A long standing interest concerns HIV reverse transcriptase where we have used structural data for the design of novel non-nucleoside inhibitors drugs and for delineating the structural basis of the escape mutants generating drug resistance. For understanding structure-function relationships of regulators we have determined structures of eukaryotic proteins such as NmrA-AreA and CC3, again by the use of crystallography.
Recent publications
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Crystal structure of the dimer of two essential Salmonella typhimurium proteins, YgjD & YeaZ and calorimetric evidence for the formation of a ternary YgjD-YeaZ-YjeE complex.
Journal article
Nichols CE. et al, (2013), Protein Sci, 22, 628 - 640
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Structures of respiratory syncytial virus nucleocapsid protein from two crystal forms: details of potential packing interactions in the native helical form.
Journal article
El Omari K. et al, (2011), Acta Crystallogr Sect F Struct Biol Cryst Commun, 67, 1179 - 1183
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Structures of respiratory syncytial virus nucleocapsid protein from two crystal forms: Details of potential packing interactions in the native helical form
Journal article
El Omari K. et al, (2011), Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 67, 1179 - 1183
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Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351
Journal article
Stamp AL. et al, (2011), Proteins: Structure, Function and Bioinformatics, 79, 2352 - 2357
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Crystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351.
Journal article
Stamp AL. et al, (2011), Proteins, 79, 2352 - 2357