Figure 4.
Figure 4. Location of important areas on ICAM-4 that mediate adhesion to αV integrins. Molecular model of ICAM-4 displayed in 3 orientations 120 degrees to one another. Residues within the ABE face are colored yellow and those in the CFG face green. (A) Residues that when mutated cause a decrease in adhesion to αV integrins are depicted in red and the super-adhesive residues in blue (i, F18; ii, W19; iii, V20; iv, R92; v, A94; vi, T95; vii, S96; viii, R97; ix, W66; x, K118; xi, N160; and xii, T162). (B) The sections of the A, G, F, and D strands of domain 1 that comprise the sequence of the peptides SVPFWVRMS (FWV) residues 15-23 (blue), TRWATSRIT (ATSR) residues 91-99 (magenta), AWSSLAHCL (AWSS) residues 76-84 (white), and RQGKTLRGP (Cpep) residues 56-64 (purple).

Location of important areas on ICAM-4 that mediate adhesion to αV integrins. Molecular model of ICAM-4 displayed in 3 orientations 120 degrees to one another. Residues within the ABE face are colored yellow and those in the CFG face green. (A) Residues that when mutated cause a decrease in adhesion to αV integrins are depicted in red and the super-adhesive residues in blue (i, F18; ii, W19; iii, V20; iv, R92; v, A94; vi, T95; vii, S96; viii, R97; ix, W66; x, K118; xi, N160; and xii, T162). (B) The sections of the A, G, F, and D strands of domain 1 that comprise the sequence of the peptides SVPFWVRMS (FWV) residues 15-23 (blue), TRWATSRIT (ATSR) residues 91-99 (magenta), AWSSLAHCL (AWSS) residues 76-84 (white), and RQGKTLRGP (Cpep) residues 56-64 (purple).

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