Obiettivo
An efficient expression system in E. coli for the production of ML1 protein for use in maintaining a future supply of crystals for analysis of the native protein and derivatives, designed to probe the enzyme (A-chain) and lectin (B-chain) activities of the protein, will be designed. This will also enable engineered mutants to be designed and produced for exploitation and development of therapeutic drugs.
The best possible simulated structure models of the A- and B-chains, based on the structure of the homologous protein ricin and known amino acid sequence data, using state-of-the-art software will be developed. These models will provide useful preliminary data on both the enzyme active site of the A-chain and the sugar binding sites of the B-chain and will also enable the hydrophobic regions of the molecule to be mapped. The models will be invaluable for molecular replacement crystal structure determination of the native protein.
Argomento(i)
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Data not availableMeccanismo di finanziamento
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WC1E 7HX London
Regno Unito