The mechanism proposed for anti-inflammatory properties of rBmAsnRS in colitis is derived from two findings: (1) the NMR structure of the 81 amino acid N terminus of rBmAsnRS showed that it folds in such a way as to mimic the way IL-8 binds to its receptor [14,15], and (2) the N terminal IL-8 like domain of rBmAsnRS is attached by a 33 amino acid flexible linker to a large catalytic region (448 amino acids) that may act as a high molecular weight “anchor” to alter cell surface receptor kinetics, receptor internalization and subsequent gene expression. The gene discussed is CXCL8; the disease is colitis.