EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
4.6.1.18 | additional information | substitution of P114 with residues that strongly prefer a trans peptide bond, like Ala, Gly, results in significant population of the C-terminal domain-swapped dimer under near-physiological conditions of pH 8.0 and 37°C. This is in stark contrast to dimerization of wild-type RNase A, which requires incubation under extreme conditions such as lyophilization from acetic acid or elevated temperature | Bos taurus |
4.6.1.18 | P114A | site-directed mutagenesis, the mutant adopts a trans conformation in contrast to the wild-type which shows a cis conformation | Bos taurus |
4.6.1.18 | P114G | site-directed mutagenesis, the mutant adopts a trans conformation in contrast to the wild-type which shows a cis conformation | Bos taurus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.6.1.18 | Bos taurus | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
4.6.1.18 | commercial preparation | - |
Bos taurus | - |
4.6.1.18 | pancreas | - |
Bos taurus | - |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.6.1.18 | ribonuclease A | - |
Bos taurus |
4.6.1.18 | RNase A | - |
Bos taurus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
4.6.1.18 | additional information | domain swapping, the process in which a structural unit is exchanged between monomers to create a dimer containing two versions of the monomeric fold, is believed to be an important mechanism for oligomerization and the formation of amyloid fibrils. In RNase residue P114 acts as a conformational gatekeeper, regulating interconversion between monomer and domain-swapped dimer forms, with cis and trans conformation, isomerization at P114 may facilitate population of a partially unfolded intermediate or alternative structure competent for domain swapping, overview | Bos taurus |