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. 1979 Jul;76(7):3218–3222. doi: 10.1073/pnas.76.7.3218

Favin versus concanavalin A: Circularly permuted amino acid sequences

Bruce A Cunningham 1, John J Hemperly 1, Thomas P Hopp 1, Gerald M Edelman 1
PMCID: PMC383795  PMID: 16592676

Abstract

We have determined the tentative amino acid sequence of the β chain (Mr 20,000) of the lectin favin. In previous studies, we have shown that the α chain (Mr 5600) of this lectin is homologous to a region in the middle of the concanavalin A (Con A) sequence (residues 70-119). Now we present evidence that the β chain is homologous to two discrete segments of Con A. The homology begins at residue 120 of Con A, extends to the COOH terminus (residue 237) and continues without interruption through the NH2-terminal 69 residues of Con A. Together, the α and β chains of favin account for a polypeptide chain equivalent in size to that of Con A. The comparison of the two proteins thus reveals a circular permutation of extensive homologous sequences. The favin molecule contains residues identical to many of the residues postulated to be involved in sugar binding by Con A, and contains all of the direct metal ligands as well as residues homologous to most of the residues that form the β-pleated sheets of Con A. These homologies suggest that the three-dimensional structures of the two lectins are likely to be very similar. Moreover, favin appears to be even more closely related in primary structure and sugar specificity to the lectins from pea and lentil, raising the possibility that all of these lectins may have structures that resemble Con A. Some of these similarities may also extend to the lectins from soybean, peanut, and red kidney bean, which have different sugar specificities but share sequence homologies with the favin β chain.

Keywords: lectins, three-dimensional structure, sequence homology, carbohydrate

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Selected References

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

  1. Allen A. K., Desai N. N., Neuberger A. Purification of the glycoprotein lectin from the broad bean (Vicia faba) and a comparison of its properties with lectins of similar specificity. Biochem J. 1976 Apr 1;155(1):127–135. doi: 10.1042/bj1550127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Becker J. W., Reeke G. N., Jr, Cunningham B. A., Edelman G. M. New evidence on the location of the saccharide-binding site of concanavalin A. Nature. 1976 Feb 5;259(5542):406–409. doi: 10.1038/259406a0. [DOI] [PubMed] [Google Scholar]
  3. Becker J. W., Reeke G. N., Jr, Wang J. L., Cunningham B. A., Edelman G. M. The covalent and three-dimensional structure of concanavalin A. III. Structure of the monomer and its interactions with metals and saccharides. J Biol Chem. 1975 Feb 25;250(4):1513–1524. [PubMed] [Google Scholar]
  4. Bornstein P., Balian G. Cleavage at Asn-Gly bonds with hydroxylamine. Methods Enzymol. 1977;47:132–145. doi: 10.1016/0076-6879(77)47016-2. [DOI] [PubMed] [Google Scholar]
  5. Cunningham B. A., Wang J. L., Waxdal M. J., Edelman G. M. The covalent and three-dimensional structure of concanavalin A. II. Amino acid sequence of cyanogen bromide fragment F3. J Biol Chem. 1975 Feb 25;250(4):1503–1512. [PubMed] [Google Scholar]
  6. Edelman G. M., Cunningham B. A., Reeke G. N., Jr, Becker J. W., Waxdal M. J., Wang J. L. The covalent and three-dimensional structure of concanavalin A. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2580–2584. doi: 10.1073/pnas.69.9.2580. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Edelman G. M. Surface modulation in cell recognition and cell growth. Science. 1976 Apr 16;192(4236):218–226. doi: 10.1126/science.769162. [DOI] [PubMed] [Google Scholar]
  8. Foriers A., Wuilmart C., Sharon N., Strosberg A. D. Extensive sequence homologies among lectins from leguminous plants. Biochem Biophys Res Commun. 1977 Apr 25;75(4):980–986. doi: 10.1016/0006-291x(77)91478-4. [DOI] [PubMed] [Google Scholar]
  9. Foriers A., de Neve R., Kanarek L., Strosberg A. D. Common ancestor for concanavalin A and lentil lectin? Proc Natl Acad Sci U S A. 1978 Mar;75(3):1136–1139. doi: 10.1073/pnas.75.3.1136. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hardman K. D., Ainsworth C. F. Structure of concanavalin A at 2.4-A resolution. Biochemistry. 1972 Dec 19;11(26):4910–4919. doi: 10.1021/bi00776a006. [DOI] [PubMed] [Google Scholar]
  11. Hardman K. D., Ainsworth C. F. Structure of the concanavalin A-methyl alpha-D-mannopyranoside complex at 6-A resolution. Biochemistry. 1976 Mar 9;15(5):1120–1128. doi: 10.1021/bi00650a026. [DOI] [PubMed] [Google Scholar]
  12. Kalb A. J., Lustig A. The molecular weight of concanavalin A. Biochim Biophys Acta. 1968 Oct 21;168(2):366–367. doi: 10.1016/0005-2795(68)90161-x. [DOI] [PubMed] [Google Scholar]
  13. Miller J. B., Hsu R., Heinrikson R., Yachnin S. Extensive homology between the subunits of the phytohemagglutinin mitogenic proteins derived from Phaseolus vulgaris. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1388–1391. doi: 10.1073/pnas.72.4.1388. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Milstein C., Milstein C. P., Feinstein A. Non-allelic nature of the basic sequences of normal immunoglobulin K chains. Nature. 1969 Jan 11;221(5176):151–154. doi: 10.1038/221151a0. [DOI] [PubMed] [Google Scholar]
  15. Porter W. H. Application of nitrous acid deamination of hexosamines to the simultaneous GLC determination of neutral and amino sugars in glycoproteins. Anal Biochem. 1975 Jan;63(1):27–43. doi: 10.1016/0003-2697(75)90186-4. [DOI] [PubMed] [Google Scholar]
  16. Reeke G. N., Jr, Becker J. W., Edelman G. M. The covalent and three-dimensional structure of concanavalin A. IV. Atomic coordinates, hydrogen bonding, and quaternary structure. J Biol Chem. 1975 Feb 25;250(4):1525–1547. [PubMed] [Google Scholar]
  17. Richardson C., Behnke W. D., Freisheim J. H., Blumenthal K. M. The complete amino acid sequence of the alpha-subunit of pea lectin, Pisum sativum. Biochim Biophys Acta. 1978 Dec 20;537(2):310–319. doi: 10.1016/0005-2795(78)90514-7. [DOI] [PubMed] [Google Scholar]
  18. SCHWARTZ J. H., EDELMAN G. M. Comparisons of Bence-Jones proteins and L polypeptide chains of myeloma globulins after hydrolysis with trypsin. J Exp Med. 1963 Jul;118:41–53. doi: 10.1084/jem.118.1.41. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Wang J. L., Becker J. W., Reeke G. N., Jr, Edelman G. M. Favin, a crystalline lectin from Vicia faba. J Mol Biol. 1974 Sep 5;88(1):259–262. doi: 10.1016/0022-2836(74)90309-x. [DOI] [PubMed] [Google Scholar]
  20. Wang J. L., Cunningham B. A., Edelman G. M. Unusual fragments in the subunit structure of concanavalin A. Proc Natl Acad Sci U S A. 1971 Jun;68(6):1130–1134. doi: 10.1073/pnas.68.6.1130. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Wang J. L., Cunningham B. A., Waxdal M. J., Edelman G. M. The covalent and three-dimensional structural of concanavalin A. I. Amino acid sequence of cyanogen bromide fragments F1 and F2. J Biol Chem. 1975 Feb 25;250(4):1490–1502. [PubMed] [Google Scholar]
  22. van Driessche E., Foriers A., Strosberg A. D., Kanarek L. N-terminal sequences of the alpha and beta subunits of the lectin from the garden pea (Pisum sativum). FEBS Lett. 1976 Dec 1;71(2):220–222. doi: 10.1016/0014-5793(76)80936-2. [DOI] [PubMed] [Google Scholar]

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