Insight into small molecule binding to the neonatal Fc receptor by X-ray crystallography and 100 kHz magic-angle-spinning NMR
Fig 6
CSPs cluster at the potential FcRnECD diprotomer interface.
(A) CSPs in surface representation of the FcRnECD diprotomer crystal structure in complex with UCB-FcRn-303 (red), with the same color-coding as in Fig 5. (B) For orientation, the FcRnECD crystal structure is shown in cartoon representation with β2m in green and dark grey and the α-chain molecules in blue and light grey. (C) The IgG and HSA interaction sites are depicted in purple and orange, respectively. The highlighted residues are discussed in the text. CSP, chemical-shift perturbation; FcRn, neonatal Fc receptor; FcRnECD, extracellular domain of the neonatal Fc receptor; HSA, Human Serum Albumin; IgG, Immunoglobulin G.