作者: Peter M. Colman , Johann Deisenhofer , Robert Huber , Walter Palm
DOI: 10.1016/S0022-2836(76)80062-9
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摘要: An electron density map at 5 A resolution of the human myeloma protein Kol (immunoglobulin G1) is reported. The describing Fab‡ fragments has been interpreted in terms known structures a V K fragment, Rei (Epp et al. , 1974), and mouse McPC603 Fab fragment (Segal 1974). It shows 'a quaternary structure different from previously reported provides evidence for flexibility switch peptides between variable constant domains on heavy light chains. No interpretable found C-terminal to inter-heavy chain disulphide bonds, forcing conclusion that Fc disordered crystal lattice implying residues immediately preceding C H2 domain. only not described by linking two arms one molecule across 2-fold symmetry axis. This can be as extending far Cys-Pro-Pro-Cys peptide.