Key result
Quantitative biophysical techniques found no evidence that the sequence downstream of amino acid 505 influences binding of the measles virus polymerase foot to the N protein.
Population
Measles virus polymerase foot domain and viral N protein (amino acids 477-525)
Comparison
Quantitative biophysical techniques to examine… vs Previous binding studies using amino acids…
Design
Preclinical
Authors
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Supports single-site polymerase-N model in measles; leaves open in vivo replication roles and needs cellular validation.
The study validates the original single-site binding model for the measles virus polymerase and nucleocapsid protein, refuting claims of a secondary binding site.
Yegambaram et al. (2010) studied Measles virus. Binding of polymerase foot domain to amino acids 477-525 of N vs. Binding to amino acids 477-505 of N was evaluated on Binding affinity and influence of downstream sequence. Quantitative biophysical techniques found no evidence that the sequence downstream of amino acid 505 influences binding of the measles virus polymerase foot to the N protein.
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