Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1975 Mar;72(3):819–823. doi: 10.1073/pnas.72.3.819

Variability of three-dimensional structure in immunoglobulins.

E A Padlan, D R Davies
PMCID: PMC432411  PMID: 805424

Abstract

A comparison of various variable immunoglobulin domains demonstrates that structural variability parallels the observed frequency of amino-acid substitutions. The similarity of the structural frameworks is in good agreement with the evolutionary relationships of the chains as derived from sequence analysis.

Full text

PDF
819

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Capra J. D., Kehoe J. M. Variable region sequences of five human immunoglobulin heavy chains of the VH3 subgroup: definitive identification of four heavy chain hypervariable regions. Proc Natl Acad Sci U S A. 1974 Mar;71(3):845–848. doi: 10.1073/pnas.71.3.845. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Edelman G. M., Cunningham B. A., Gall W. E., Gottlieb P. D., Rutishauser U., Waxdal M. J. The covalent structure of an entire gammaG immunoglobulin molecule. Proc Natl Acad Sci U S A. 1969 May;63(1):78–85. doi: 10.1073/pnas.63.1.78. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Edelman G. M., Gall W. E. The antibody problem. Annu Rev Biochem. 1969;38:415–466. doi: 10.1146/annurev.bi.38.070169.002215. [DOI] [PubMed] [Google Scholar]
  4. Edelman G. M. The covalent structure of a human gamma G-immunoglobulin. XI. Functional implications. Biochemistry. 1970 Aug 4;9(16):3197–3205. doi: 10.1021/bi00818a012. [DOI] [PubMed] [Google Scholar]
  5. Epp O., Colman P., Fehlhammer H., Bode W., Schiffer M., Huber R., Palm W. Crystal and molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI. Eur J Biochem. 1974 Jun 15;45(2):513–524. doi: 10.1111/j.1432-1033.1974.tb03576.x. [DOI] [PubMed] [Google Scholar]
  6. Kabat E. A., Wu T. T. Attempts to locate complementarity-determining residues in the variable positions of light and heavy chains. Ann N Y Acad Sci. 1971 Dec 31;190:382–393. doi: 10.1111/j.1749-6632.1971.tb13550.x. [DOI] [PubMed] [Google Scholar]
  7. Phillips D. C. The development of crystallographic enzymology. Biochem Soc Symp. 1970;30:11–28. [PubMed] [Google Scholar]
  8. Poljak R. J., Amzel L. M., Avey H. P., Chen B. L., Phizackerley R. P., Saul F. Three-dimensional structure of the Fab' fragment of a human immunoglobulin at 2,8-A resolution. Proc Natl Acad Sci U S A. 1973 Dec;70(12):3305–3310. doi: 10.1073/pnas.70.12.3305. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Rossman M. G., Liljas A. Letter: Recognition of structural domains in globular proteins. J Mol Biol. 1974 May 5;85(1):177–181. doi: 10.1016/0022-2836(74)90136-3. [DOI] [PubMed] [Google Scholar]
  10. Rudikoff S., Potter M. Variable region sequence of the heavy chain from a phosphorylcholine binding myeloma protein. Biochemistry. 1974 Sep 10;13(19):4033–4038. doi: 10.1021/bi00716a034. [DOI] [PubMed] [Google Scholar]
  11. Schiffer M., Girling R. L., Ely K. R., Edmundson A. B. Structure of a lambda-type Bence-Jones protein at 3.5-A resolution. Biochemistry. 1973 Nov 6;12(23):4620–4631. doi: 10.1021/bi00747a013. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Wu T. T., Kabat E. A. An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity. J Exp Med. 1970 Aug 1;132(2):211–250. doi: 10.1084/jem.132.2.211. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES