The structural analysis of the Fab' fragment of human myeloma immunoglobulin IgGl(λ) New was extended to a nominal resolution of 2.0 Å. Each of the structural subunits corresponding to the variable and to the constant homology regions of the light and heavy chains contains 2 irregular β sheets which are roughly parallel to each other and surround a tightly packed interior of hydrophobic side chains. About 50-60% of the amino acid residues are included in β pleated sheets. Sequence alignments between the homology regions of Fab' New obtained by comparison of their 3 dimensional structures are given. Some of the sequence variations observed in light and heavy chains and the role of the regions of hypervariable sequence in defining the size and shape of the active site of different immunoglobulin molecules are discussed on the basis of the 3 dimensional model of Fab' New.
|Original language||English (US)|
|Number of pages||5|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - 1974|
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