Designing Stable Structures of Leishmania major Small Hydrophilic Endoplasmic Reticulum associated Protein: templates for Antibody Production and Rational Drug Design

Doctor Robert William Janes (primary)
School of Biological and Chemical Sciences
Queen Mary
Professor Bonnie Ann Wallace (secondary)
Biological Sciences


Intrinsically disordered proteins, such as Small Hydrophilic Endoplasmic Reticulum-associated Protein (SHERP) from Leishmania major, are becoming associated with many disease states. While not having a regular solution structure, an active structure only forms when binding to its key site of action. This structure is the perfect target for developing antibodies and for rational drug design, however, it exists for a fleeting period of time making it almost inaccessible as a target. The project aims are to generate a stable active structure form of SHERP capable of use as a template for creating antibodies and for rational drug design.


Drew, E. and Janes, R.W. (2019) 2StrucCompare: a webserver for visualizing small but noteworthy differences between protein tertiary structures through interrogation of the secondary structure content. Nucleic Acids Research,

Drew, E, Jones, D., Wallace, B.A. (2018) Protein Design for Decreased Disorder. SHERP as an Exemplar Protein Biophysical Journal 110: 555a.

Moore, B. Miles, A.J., Guerra, C.G., Simpson, P., Iwata, M., Wallace, B.A., Matthews, S.J., Smith, D.F., and Brown, K.A. (2010) Structural Basis of Molecular Recognition by SHERP at Membrane Surfaces. J. Biol. Chem. 286:9246-9256.

Molecules, cells and industrial biotechnology
Area of Biology
BiotechnologyStructural Biology
Techniques & Approaches
BiochemistryBioinformaticsBiophysicsChemistryMolecular BiologySimulation / Modelling