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Literature summary for 4.6.1.18 extracted from

  • Miller, K.H.; Karr, J.R.; Marqusee, S.
    A hinge region cis-proline in ribonuclease A acts as a conformational gatekeeper for C-terminal domain swapping (2010), J. Mol. Biol., 400, 567-578.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 4.6.1.18

Protein Variants

Protein Variants Comment Organism
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
P114A site-directed mutagenesis, the mutant adopts a trans conformation in contrast to the wild-type which shows a cis conformation Bos taurus
P114G site-directed mutagenesis, the mutant adopts a trans conformation in contrast to the wild-type which shows a cis conformation Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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 Bos taurus
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pancreas
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 Bos taurus
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Synonyms

Synonyms Comment Organism
ribonuclease A
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 Bos taurus
RNase A
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 Bos taurus

General Information

General Information Comment Organism
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