In cell motility group, S100A2, a calcium-binding protein, which had pronouncedly 1.8-fold higher expression in high-invasive KKU-M213 cells, has been identified.
Furthermore, vertebrate NPC2 has a similar binding fold as MD-2 (a lipopolysaccharide-binding protein), which is indispensable for toll-like (TLR4) receptor signaling in the vertebrate immune system [ 55].
A domain covering repeats of ∼50 amino acids containing conserved residues, which folds into a β-propeller secondary structure, first identified in kelch proteins and found in several actin-binding proteins.
Within mitochondria are a multitude of proteins, which must be folded properly to function.
Proteins, which are strings of amino acids, fold into distinct shapes to carry out various functions in the body.
Structural analysis of semi-specific oligosaccharide recognition by a cellulose-binding protein of thermotoga maritima reveals adaptations for functional diversification of the oligopeptide periplasmic binding protein fold.
These findings are combined with the up-regulation of IL18 binding protein (IL18BP, 8-fold at 6-hpi) which sequesters IL18, further inhibiting IL18 and IFN-γ production and also with the up-regulation of the canonical Th2 marker, IL13 (20-fold at 6 hpi).
But these proteins, which begin as long strings, have to fold into very specific shapes to do their job.
The determination of the SMU.440 crystal structure revealed a cavity which is similar to that of hormone and especially polyketide binding proteins sharing the same fold, indicating a polyketide-like binding site in SMU.440 homologs.
Such similar patches are often related to ligand binding and the search for them exploits the fact that binding sites share similar patterns of interactions in proteins which perform similar functions but may or may not have different folding patterns.
