Literature summary for 4.6.1.18 extracted from

Miller, K.H.; Marqusee, S.
Propensity for C-terminal domain swapping correlates with increased regional flexibility in the C-terminus of RNase A (2011), Protein Sci., 20, 1735-1744.

Search for more literature for 4.6.1.18

Protein Variants

Protein Variants	Comment	Organism
H119A	active-site mutation	Bos taurus
H119A/P114G	site-directed mutagenesis	Bos taurus
H119A/P93A	site-directed mutagenesis	Bos taurus
additional information	two RNase A variants, P114G and P93A, have the same global stability yet very different domain-swapping propensity, differences in protection factors suggest differential local dynamics	Bos taurus
P114G	site-directed mutagenesis, the mutant adopts a trans conformation in contrast to the wild-type who shows a cis conformation. The P114G mutant readily domain swaps under physiological conditions in contrast to the wild-type enzyme. The P114G variant has decreased protection from hydrogen exchange compared to the wild-type protein near the C-terminal hinge region. Structure of RNase A P114G with HX fluctuation, overview	Bos taurus
P93A	site-directed mutagenesis	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Subunits

Subunits	Comment	Organism
monomer	primarily	Bos taurus

Synonyms

Synonyms	Comment	Organism
pancreatic ribonuclease A	-	Bos taurus
RNase A	-	Bos taurus

General Information

General Information	Comment	Organism
additional information	pancreatic ribonuclease A shows domain swapping, a type of oligomerization in which monomeric proteins exchange a structural element, resulting in oligomers whose subunits recapitulate the native, monomeric fold, under extreme conditions, such as lyophilization from acetic acid. The major domain swaps dimer form of RNase A exchanges a beta-strand at its C-terminus to form a C-terminal domain-swapped dimer, mechanism, overview. Domain swapping occurs via a local high-energy fluctuation at the C-terminus	Bos taurus

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Release 2023.1 (January 2023)