Figure 4.
Cryo-EM structures of R21D10 Fab in complex with αIIbβ3 in 2 different conformations. (A) Atomic models of the αIIbβ3-R21D10 Fab complex in 2 conformations, with legs being semiextended (left) or bent (right). Both structures are colored based on individual domains. (B) Comparison of superimposed bent (green) and semi-extended (magenta) conformations of the αIIbβ3-R21D10 Fab complexes. Both structures are shown as ribbon diagram. The bent and semiextended structures of αIIbβ3 are superimposed and colored green and magenta, respectively; the corresponding R21D10 Fab structures are colored dark green and dark magenta, respectively (top). The αIIb thigh, calf-1, and calf-2 domains in bent (green) and semiextended (magenta) conformations (middle). The β3 hybrid, PSI, and integrin-epidermal growth factor 1 (I-EGF1)-4 domains in bent (green) and semiextended (magenta) conformations (bottom). (C) Interaction between αIIbβ3 and R21D10 Fab in semiextended (top) and bent conformations (bottom). Interaction between I-EGF1 domain and R21D10 Fab (left). Interaction of the I-EGF2 domain with its surrounding area (right). Enlarged views of the interactions (boxed) are shown with individual domains colored and labeled. Each subunit participating in the interactions is depicted in a different color and labeled. Key residues involved in these interactions are shown with side chains. Propeller and thigh domains from the αIIb subunit are represented with red color, whereas βI and hybrid domains are represented with blue color. The PSI, I-EGF1, and I-EGF2 domains are shown in dark red, orange-red, and magenta, respectively. The charge interactions are indicated by dotted red lines, whereas the hydrogen bonds are indicated by dotted black lines. Dotted green lines indicate the hydrogen bonds that are lost when going back and forth between the bent and semiextended conformations. Conformational changes in the 2 loops of the I-EGF2 domain are indicated by orange and red asterisks, respectively. The loop containing the Lys514-Arg516 segment within the thigh domain is colored with cyan in both conformations.

Cryo-EM structures of R21D10 Fab in complex with αIIbβ3 in 2 different conformations. (A) Atomic models of the αIIbβ3-R21D10 Fab complex in 2 conformations, with legs being semiextended (left) or bent (right). Both structures are colored based on individual domains. (B) Comparison of superimposed bent (green) and semi-extended (magenta) conformations of the αIIbβ3-R21D10 Fab complexes. Both structures are shown as ribbon diagram. The bent and semiextended structures of αIIbβ3 are superimposed and colored green and magenta, respectively; the corresponding R21D10 Fab structures are colored dark green and dark magenta, respectively (top). The αIIb thigh, calf-1, and calf-2 domains in bent (green) and semiextended (magenta) conformations (middle). The β3 hybrid, PSI, and integrin-epidermal growth factor 1 (I-EGF1)-4 domains in bent (green) and semiextended (magenta) conformations (bottom). (C) Interaction between αIIbβ3 and R21D10 Fab in semiextended (top) and bent conformations (bottom). Interaction between I-EGF1 domain and R21D10 Fab (left). Interaction of the I-EGF2 domain with its surrounding area (right). Enlarged views of the interactions (boxed) are shown with individual domains colored and labeled. Each subunit participating in the interactions is depicted in a different color and labeled. Key residues involved in these interactions are shown with side chains. Propeller and thigh domains from the αIIb subunit are represented with red color, whereas βI and hybrid domains are represented with blue color. The PSI, I-EGF1, and I-EGF2 domains are shown in dark red, orange-red, and magenta, respectively. The charge interactions are indicated by dotted red lines, whereas the hydrogen bonds are indicated by dotted black lines. Dotted green lines indicate the hydrogen bonds that are lost when going back and forth between the bent and semiextended conformations. Conformational changes in the 2 loops of the I-EGF2 domain are indicated by orange and red asterisks, respectively. The loop containing the Lys514-Arg516 segment within the thigh domain is colored with cyan in both conformations.

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