Comparative site-directed mutagenesis in the catalytic amino acid triad in calicivirus proteases
β Scribed by Tomoichiro Oka; Kosuke Murakami; Takaji Wakita; Kazuhiko Katayama
- Book ID
- 108578488
- Publisher
- Center for Academic Publications, Japan
- Year
- 2011
- Tongue
- English
- Weight
- 283 KB
- Volume
- 55
- Category
- Article
- ISSN
- 0385-5600
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π SIMILAR VOLUMES
In the catalytic reaction of serine proteases the basicity of a histidine and the nucleophilicity of a serine, both residues together with an aspartate residue belonging to the catalytic triad, are of great importance. The influence of amino acid substitution on the basicity and the nucleophilicity
Osteopontin (OPN) is a secreted calcium-binding phosphoprotein produced in a variety of normal and pathological contexts, including tissue mineralization and cancer. OPN contains a conserved RGD (arg-gly-asp) amino acid sequence that has been implicated in binding of OPN to cell surface integrins. T