Fig. 1.
Fig. 1. Homology models of the Fc fragment of hIgG1. / The homology model has been developed using 1e4k.pdb in Brookhaven Protein Data Bank as a template.2 The modeling has been done with SwissPdbViewer and the SwissProt modeling server. The raytracing of the figure has been done using the program PovRay in SGI computer at Human Genome Center, Institute of Medical Science, the University of Tokyo. The models are superimposed onto 1e4k.pdb based on homology. Models are shown in β-strand, α-helical presentation connected with α-carbon trace. The side chains of Val158 and Phe158 are shown in space filling model. (A) Docking between FCGR3A-Val and hIgG1. (B) Docking between FCGR3A-Phe and hIgG1. (C) Details of amino acid residues close to 158F of FCGR3A-Phe molecules. The side chains of IgG1 molecule within 10Å from 158 Phe are shown in balls and sticks model.

Homology models of the Fc fragment of hIgG1.

The homology model has been developed using 1e4k.pdb in Brookhaven Protein Data Bank as a template.2 The modeling has been done with SwissPdbViewer and the SwissProt modeling server. The raytracing of the figure has been done using the program PovRay in SGI computer at Human Genome Center, Institute of Medical Science, the University of Tokyo. The models are superimposed onto 1e4k.pdb based on homology. Models are shown in β-strand, α-helical presentation connected with α-carbon trace. The side chains of Val158 and Phe158 are shown in space filling model. (A) Docking between FCGR3A-Val and hIgG1. (B) Docking between FCGR3A-Phe and hIgG1. (C) Details of amino acid residues close to 158F of FCGR3A-Phe molecules. The side chains of IgG1 molecule within 10Å from 158 Phe are shown in balls and sticks model.

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