Andersen, J. T. et al. Ligand binding and antigenic properties of a human neonatal Fc receptor with mutation of two unpaired cysteine residues.
Mutation of two of the sites, S324 and T515, partially inhibited the ability of muskelin to self-associate in cells and inhibited responsiveness to activated PKC.
Mutation of two putative phosphorylation sites in the N-terminus of KCNQ1 and one site in KCNE1 (S102) blocked the inhibition of Ang II.
It has been found that with mutation of two surface residues (Lys22 → Glu and His104 → Arg) in human purine nucleoside phosphorylase (hPNP), there is an enhancement of catalytic activity in the chemical step.
In order to explore the basis for cofactor promiscuity, structure-guided mutation of two residues in the cofactor binding site, Gln193 and His194, in SMFMO were performed in an attempt to imitate the cofactor binding site of the NADPH-dependent FMO from Methylophaga aminisulfidivorans sp. SK1 (mFMO), in which structurally homologous residues Arg234 and Thr235 bind the NADPH 2′-ribose phosphate.
In rel2 mutant, the mutation of two nucleotide substitutions in DUF630 domain led to the loss-of-function of REL2 locus and the function of REL2 could be confirmed by complementary expression of REL2 in rel2 mutant.
However, the mutation of two nucleotide substitutions in the ORF region causing amino acid substitutions (Cys3 to Tyr3, Val14 to Met14) should lead to loss of REL2 function in the mutant.
Previous homology modeling studies suggested that YfiB contains a Pal-like PG-binding site (Parsons et al., 2006), and the mutation of two residues at this site, D102 and G105, reduces the ability for biofilm formation and surface attachment (Malone et al., 2012).
This catalytic activity is abrogated by mutation of two conserved glutamate residues to aspartates (E538D and E540D) of SpvB [35].
We have previously shown that mutation of two cysteines in the sulfatase domain of each Sulf eliminated sulfatase activity [22].
Additionally, mutation of two asparagines (255/257) as well as the EN 271/272 mutation somewhat reduced activity (Figure 3B, lanes 11 and 13).
