Crystal structure of IgE complexed with E2_79, an anti-IgE inhibitor

Accelerated disassembly of IgE-receptor complexes by a disruptive macromolecular inhibitor.

IG-LIKE DOMAINS 3 AND 4, RESIDUES 210-428

0.1 M Phosphate-citrate pH 4.2, 5% (w/v) PEG-3000, 25% (v/v) 1,2-propanediol, 10% (v/v) glycerol, VAPOR DIFFUSION, HANGING DROP, temperature 298K

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE NATIVE DATA WERE SUBMITTED TO THE DIFFRACTION ANISOTROPY SERVER, WHICH INDICATED SIGNIFICANT ANISOTROPY WITH PRINCIPLE COMPONENTS OF 20.6 X 20.5 X -41.2 (ANGSTROM2) ALONG THE A*. B* AND C* AXES. THE DATA WERE TRUNCATED TO 4.2 ANGSTROM ALONG THE C* AXIS AND 4.5 ANGSTROM ALONG THE A*/B* AXES.

Protein: E2_79, Ig epsilon chain C region

One biological assembly consisting of one IgE-Fc and two E2_79 is observed in an asymmetric unit.

Ig-fold, immunity, high/low affinity receptor, IMMUNE SYSTEM-INHIBITOR complex

chain C and (resseq 333:392 or resseq 394:423 or resseq 425:426 or resseq 428:436 or resseq 438:544 )

chain D and (resseq 333:392 or resseq 394:423 or resseq 425:426 or resseq 428:436 or resseq 438:544 )