In addition, it has been shown that pathogen- or stress-derived peptides presented by the HLA-B molecule could alter the binding face of the Bw4 epitope for KIR interaction [ 33, 34].
In contrast to the Runx proteins from the cnidarians and the demosponge Amphimedon, the CBFβ binding face of the sponge Oscarella carmela Runx protein is quite distinct, with many non-conservative amino acid substitutions found both in the periphery and in the center of the CBFβ binding region.
Interestingly, the CBFβ-binding faces of the sponge proteins are more divergent.
Strikingly, all 10 residues of the DNA binding face of all of the cnidarian and sponge RD's are completely conserved with their human counterpart, strongly indicating that these proteins bind DNA in a similar manner and prefer the same DNA sequence motif.
However, the mutation introduces an additional positively charged arginine residue on the RNA-binding face of the deaminase domain very close to the active site and the DSH1 phenotype suggests that the ADAR1 G1007R protein may be catalytically inactive.
At the receptor kinase interface, the kinase protein L545W mutation (kpL545W) was designed to weaken the primary receptor kinase contact by introducing a surface Trp substitution onto the receptor-binding face of the kinase P5 regulatory domain.
Co-crystallization of the most potent analog TxIA(A10L) with Ac-AChBP identified a new α-conotoxin binding mode that was stabilized by a critical salt bridge between Arg5-TxIA(A10L) and a highly conserved Asp residue on the principal face of the binding face of Ac-AChBP.
The structure of the auto-inhibited form of PARKIN uncovered that access to the catalytic Cys431 is blocked by another domain, and in addition, that a linker helix (referred to as the repressor element of PARKIN (REP)) binds and occludes the E2 binding face of RING1 (Riley et al, 2013; Trempe et al, 2013; Wauer and Komander, 2013).
We used split-superpositive Green Fluorescent Protein (split-spGFP) reassembly to screen a 5×1010 library of resurfaced proteins that are shape complementary to the putative binding face of gankyrin and identified mutants that potently and selectively bind this oncoprotein in vitro and in living cells.
Pdar and Notch-1 exhibit ∼12% and ∼9% sequence homology, respectively, with the concave binding face of Gankyrin.
In contrast, solvent exposed residues on the putative binding face of gankyrin are primarily polar or charged.
