Abstract
A comparison of five constant region sequences of human and mouse k and lambda immunoglobulin chains has been undertaken in order to reveal sequence homologies and evolutionary relationships. Simultaneously, a comparison with the three-dimensional structure of one mouse k-chain (McPC 603) has suggested structural reasons why many of the residues are invariant or conserved along k versus lambda lines. There are a number of residues that have remained invariant despite exposed positions for reasons that do not apppear to be connected with the folding of the CL domain.
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Selected References
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- Poljak R. J., Amzel L. M., Chen B. L., Phizackerley R. P., Saul F. The three-dimensional structure of the fab' fragment of a human myeloma immunoglobulin at 2.0-angstrom resolution. Proc Natl Acad Sci U S A. 1974 Sep;71(9):3440–3444. doi: 10.1073/pnas.71.9.3440. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Segal D. M., Padlan E. A., Cohen G. H., Rudikoff S., Potter M., Davies D. R. The three-dimensional structure of a phosphorylcholine-binding mouse immunoglobulin Fab and the nature of the antigen binding site. Proc Natl Acad Sci U S A. 1974 Nov;71(11):4298–4302. doi: 10.1073/pnas.71.11.4298. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Svasti J., Milstein C. The complete amino acid sequence of a mouse kappa light chain. Biochem J. 1972 Jun;128(2):427–444. doi: 10.1042/bj1280427. [DOI] [PMC free article] [PubMed] [Google Scholar]