Table 2. Fine mapping with CLIPS-constrained peptides. Light gray boxes indicate charged residues. Values are corrected for background.
Nine single positional changes that eliminated RING-binding. The complex molecular architecture of the discontinuous binding site was maintained via fixation of linear peptides. Thus changes in binding are due to changes in individual amino acids not changes in the molecular scaffold. Candidates on this list were selected from fine mapping of CLIPS-constrained RING peptides.
Consensus sequence | Value | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P | V | I | T | H | C | ACVFAKPAIC | + | AIQNEQP | H | A | K | C | P | L | CR | |
Changes that eliminated binding | ||||||||||||||||
M | + | 3 | ||||||||||||||
R | + | 2 | ||||||||||||||
D | + | 1 | ||||||||||||||
T | + | 0 | ||||||||||||||
+ | Q | −4 | ||||||||||||||
S | + | −16 | ||||||||||||||
+ | P | −23 | ||||||||||||||
K | + | −46 | ||||||||||||||
P | + | −61 |