Stephen J Perkins

Professor of Structural Biochemistry

Based at UCL

Personal Website

Structural Immunology Group

Our major research interests lie in solution structural determinations of proteins and their interactions in the immune system, primarily involving the complement proteins and antibodies. Our major technologies include small angle X-ray and neutron solution scattering at the ESRF, Diamond, ISIS and ILL (SAXS, SANS) and analytical ultracentrifugation (AUC) on our two Beckman XL-I analytical ultracentrifuges, one of which is equipped with fluorescent optics. We also possess surface plasmon resonance and dual polarization interferometry instruments that help with our interactions studies, access protein crystallography through collaborations, and maintain web sites that detail the variants and phenotypes in mutant complement and coagulation proteins. In the UK, we head the CCP-SAS project, a joint US/UK collaborative open-source software development project that provides the infrastructure and tools for analysing small angle scattering data on complex systems using atomistic and coarse grained modelling approaches (see

Our recent antibody results include the molecular dynamics modelling of human IgA1 antibody based on SAXS and SANS data which provided the most detailed view of its solution structure to date, and clarified its binding to its FcαR receptor (Hui et al., 2015). Similar analyses were performed for the human IgG1 and IgG4 subclasses that accounted for their different immune reactivities (Rayner et al., 2014, 2015).

Our most recent complement results from molecular dynamics modelling of SAXS data include the demonstration of significant flexibility in MASP, C4b and collagen that are relevant to lectin pathway activation (Fung et al., 2016; Nan et al., 2017, Walker et al., 2017).

Selected publications

Flexibility in mannan-binding lectin-associated serine proteases-1 and -2 provides novel insight on lectin pathway activation
Nan, R., Furze, C.M., Wright, D.W., Gor, J., Wallis, R., Perkins, S.J. 
Structure (2017) 25 (2):364-375
The solution structures of native and patient monomeric human IgA1 reveal asymmetric extended structures: implications for function and IgAN disease
Hui, G.K., Wright, D.W., Vennard, O.L., Rayner, L.E., Pang, M., Yeo, S.C., Gor, J., Molyneux, K., Barratt, J., Perkins, S.J.
Biochemical Journal (2015) 471 (2):255-265
Atomistic modelling of scattering data in the Collaborative Computational Project for Small Angle Scattering (CCP-SAS)
Perkins, S.J., Wright, D.W., Zhang, H., Brookes, E.H., Chen, J., Irving, T.C., Krueger, S., Barlow, D.J., Edler, K.J., Scott, D.J., Terrill, N.J., King, S.M., Butler, P.D., Curtis, J.E.
Journal of Applied Crystallography (2016) 49 (Pt 6):1861-1875