Abstract:
:The 3-D complex structures of extracellular domain of human CD16 (FcgammaRIII) and hIgG1 or B88-9 were obtained by means of computer-guided molecular modeling, respectively. The binding epitopes were predicted and binding energy was calculated theoretically. The epitopes of human CD16 interacted with hIgG1 and B88-9 were different and the binding energy of B88-9 was stronger than hIgG1. The computer competing simulation results showed that B88-9 could bind to CD16 when CD16 was also bound by hIgG1, while IgG1 could not bind to CD16 after CD16 was bound by B88-9. By flow cytometry analysis, the competitive binding activity of B88-9 to CD16 with hIgG1 was evaluated. With the increasing concentrations of hIgG1, the binding activity of B88-9 was not interfered markedly. It suggested that hIgG1 could not inhibit the interaction of CD16 and B88-9 and the binding domain of hIgG1 and B88-9 on CD16 was different.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Feng J,Xie Z,Yu M,Guo N,Shen Bdoi
10.1016/j.molimm.2004.03.024subject
Has Abstractpub_date
2004-05-01 00:00:00pages
93-8issue
1eissn
0161-5890issn
1872-9142pii
S0161589004000872journal_volume
41pub_type
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