Three-Dimensional Structure of the Fab′ Fragment of a Human Immunoglobulin at 2.8- Resolution
摘要：
The structure of the Fab′fragment of a human myeloma immunoglobulin was determined by x-ray crystallographic analysis at 2.8- angstrom resolution. The Fourier map of the electron density was correlated with the aminoacid sequence to obtain a three-dimensional model. Four globular subunits, which correspond to the homology regions of the light and heavy chains, are arranged in a tetrahedral configuration. These subunits closely resemble each other, sharing a basic pattern of polypeptide chain folding. In each subunit, long sequences of tightly packed, hydrogen bonded polypeptide chain run parallel to the major axis of the subunit. No helical conformation can be seen. Different patterns of interchain disulfide linkage and unusual intrachain disulfide bonds that have been observed in other immunoglobulins can be explained with this model. The regions of hypervariable sequences in the light and heavy chains occur at one end of the molecule, in close spatial proximity.
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DOI：
10.1073/pnas.70.12.3305
被引量：
年份：
1973
Wiley
Semantic Scholar
万方医学
万方医学
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