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Structural similarity of the antigen-binding sites of VH5-51 encoded anti-V3 mAbs.

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posted on 02.12.2011, 01:52 by Miroslaw K. Gorny, Jared Sampson, Huiguang Li, Xunqing Jiang, Maxim Totrov, Xiao-Hong Wang, Constance Williams, Timothy O'Neal, Barbara Volsky, Liuzhe Li, Timothy Cardozo, Phillipe Nyambi, Susan Zolla-Pazner, Xiang-Peng Kong

(A) A structural superimposition of the Cα atoms of the Fab variable domains of complexes 1006/MN (green), 2219/MN (cyan), 2557/NY5 (magenta), 2558/MN (yellow), and 4025/ConA (salmon). Note the domains of CDR H1, H2, L1 and L2 superimposed well, while that of CDR L3 and H3 is more structurally divergent. (B) Same superimposition as that in panel (A) but with the key contact residues of the mAbs labeled (all contact residues are shown in Tables 4 and 5). The position of the V3 is illustrated as a dashed line. (C) and (D) Structural details of the antigen combining sites of the light (C) and heavy chains (D) in the five complexes.

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