Supplemental materials for: McEwan et al
Files in this Data Supplement:
- Document 1. Supplemental table and figures (PDF, 103 KB)
- Video 1. An animation of the refined GPIbβE1.25-Å electron density map is shown (blue) with SigmaA m2Fo-DFc coefficients and phases Φc contoured at 1.5 r.m.s (REFMAC) (WMV, 4.81 MB) -
Residues around the area of residue Tyr88 are shown as stick in orange similar to the depiction in Fig. 1C.
- Video 2. An animated model of the GPIbβE topology (as in Fig. 2A) with residues Cys5, Arg17, Pro29, Asn64, Pro74, Tyr88, Pro96, and Ala108 affect by BSS mutations shown as stick in green (exposed) and red (buried) (WMV, 2.38 MB)
- Video 3. An animated model of the GPIbβEabc tetramer topology diagram (as shown in Fig. 4A) (WMV, 2.42 MB) -
This illustrates front and side views of the structure showing the C-termini (blue) are brought into proximity on one face of the structure. Key interfacial residue Tyr 106 is illustrated as stick colored in green.
- Video 4. An animation of the model of the membrane-proximal portion of the GPIb-IX complex as shown in Fig. 7A (WMV, 2.33 MB) -
This illustrates the GPIbα chain TM domain (in green) extending towards the N-terminus (top), GPIbβ ectodomain and TM domain (in sky blue and dark blue), and GPIX ectodomain and TM domain (in purple). Tyr106 from GPIbβ is shown as stick. Interchain disulphides are shown as stick (yellow). Residues affected by GPIbβ BSS mutations are shown in stick as red for Ala108 and Pro74.