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. 2023 Aug 4;299(10):105136. doi: 10.1016/j.jbc.2023.105136

Figure 3.

Figure 3

Conformational changes in open B∗37:01/β2m induced by interaction with chTapasin.A, 2D 1H-13C SOFAST HMQC spectra of U-[15N, 2H], 13CH3-labeled alanine, isoleucine, leucine, and valine residues of human β2m (H31C) in the B∗37:01 (G120C)-FEDLRVJSF bound state (in red). The sample was subsequently incubated with chicken Tapasin and UV irradiated for 40 min prior to collecting additional 1H-13C SOFAST HMQC spectra (in cyan). Both spectra were collected at 600 MHz 1H magnetic field, at 25 °C. Due to lack of stereospecific assignments, the CD1 and CD2 methyl groups of Leu54 are not indicated. B–D, Zoomed regions of the 1H-13C SOFAST HMQC spectra with arrows highlighting methyl probes experiencing minor chemical shift changes upon chTapasin binding, indicated by a slow-exchanging minor state peak. E, Methyl probes that show a detectable slow-exchanging minor peak upon chTapasin binding are shown as red spheres on the predicted B∗37:01/β2m/chTapasin model by BAKER-ROBETTA (29).