Solution structures of the immunologically important proteins IgA, C3 and IgG

DOI

Abnormally glycosylated IgA leads to IgA nephropathy, the most common cause of renal failure. IgG antibody represents one-third of new drugs currently in development, and its conformational stability under various conditions is essential for biopharmaceuticals. We will identify the solution structures of human IgA and IgG in a range of buffers. We will apply our powerful constrained scattering modelling approach to reveal conformational changes in these antibodies that are crucial to disease and biotechnology. We are also investigating the solution structures of complexes formed between the major complement regulator factor H and its target C3b. Complement C3 undergo large conformational changes to form C3b, which shows different domain arrangements for C3b in its crystal structures. We will identify the C3b solution structure to clarify its mechanism of action.

Identifier
DOI https://doi.org/10.5286/ISIS.E.24089952
Metadata Access https://icatisis.esc.rl.ac.uk/oaipmh/request?verb=GetRecord&metadataPrefix=oai_datacite&identifier=oai:icatisis.esc.rl.ac.uk:inv/24089952
Provenance
Creator Professor Stephen Perkins; Mr Owen Vennard; Ms Lucy Rayner; Miss Elizabeth Rodriguez
Publisher ISIS Neutron and Muon Source
Publication Year 2015
Rights CC-BY Attribution 4.0 International; https://creativecommons.org/licenses/by/4.0/
OpenAccess true
Contact isisdata(at)stfc.ac.uk
Representation
Resource Type Dataset
Discipline Photon- and Neutron Geosciences
Temporal Coverage Begin 2012-12-14T03:42:39Z
Temporal Coverage End 2012-12-16T09:00:31Z