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. Author manuscript; available in PMC: 2006 Aug 30.
Published in final edited form as: J Thromb Haemost. 2005 Dec;3(12):2764–2772. doi: 10.1111/j.1538-7836.2005.01618.x

Fig. 4.

Fig. 4

Model of the interface between blade 2 of the αIIbβ-propeller and βA domain of β3. Blade 2 of the αIIbβ-propeller (PDB 1TXV) shown in black are the six amino acids that are deleted in the Palestinian mutation. Trp110 of αIIb and Arg261 of β3 are shown as balls (A). Also depicted are Cys107 and Cys130 that are normally juxtaposed by disulfide bond and predictably are disrupted by replacing Cys107 by Ser. Note that the contact between Trp110 and Arg261 is disrupted when Trp110 is replaced by Ala (B). The figure was made using RasMol program and was based on the crystal structure of αIIbβ3 [10].