Kappa chain structure from a crystallized murine Fab′: Role of joining segment in hapten binding
1981; Elsevier BV; Volume: 18; Issue: 8 Linguagem: Inglês
10.1016/0161-5890(81)90062-6
ISSN1872-9142
AutoresStuart Rudikoff, Yoshinori Satow, Eduardo A. Padlan, Daryl L. Davies, Michael Potter,
Tópico(s)Glycosylation and Glycoproteins Research
ResumoThe entire variable region sequence of the kappa chain from M603, a phosphorylcholine(PC)-binding myeloma protein has been determined. This structure is of particular interest in that the Fab' fragment from M603 has been crystallized and its three-dimensional structure determined. Analysis of the light-chain amino acid sequence has permitted identification of specific residues involved in light-heavy chain and light chain-hapten interactions. Position 96 (Leu) was found to be a hapten-contacting amino acid. This residue is not encoded in the variable region gene but rather in the ‘joining’ gene which encodes amino acids 96–108. When the M603 sequence was compared to that of a second PC-binding myeloma protein M 167, these structures were found to differ by 31% in their framework segments and 62% in complementarity-determining regions. Both light chains have Leu at position 96 and use the same joining segment sequence as apparently does a third PC-binding protein H8. These results suggest that Leu at position 96 and this particular joining segment sequence may be required in PC-binding antibodies.
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