PMID: 7822104Sep 1, 1994Paper

Amino acid sequence and properties of vasopressin-associated elephant neurophysin

International Journal of Peptide and Protein Research
H HuangE Breslow

Abstract

The primary structure of an elephant neurophysin, homologous to vasopressin-associated neurophysins, is reported. The protein contains a Tyr for Asn substitution at position 75, a position in direct contact with residues 77 and 78 of the monomer-monomer interface. This Tyr residue therefore serves as a potential reporter of the path involved in the long-range linkage between peptide binding and dimerization in this system. NMR studies of the protein in unliganded and liganded states demonstrated normal dimerization properties and the expected increase in dimerization associated with binding peptide. In keeping with an elevated pKa of 11.1 assigned to Tyr-75 by UV spectrophotometric titration, the NMR signals from the 3,5 and 2,6 ring protons of Tyr-75 were shifted 0.3 and 0.2 ppm upfield, respectively, relative to their positions in small peptides, indicating significant shielding and/or hydrogen bonding. The Tyr-75 ring proton signals narrowed slightly, with no discernible change in chemical shift, on conversion from dimer to monomer in the unliganded state. Ring protons of Tyr-49, distant from the monomer-monomer interface, but adjacent to the peptide-binding site, were markedly perturbed by dimerization, in accord with their...Continue Reading

References

May 15, 1992·Proceedings of the National Academy of Sciences of the United States of America·R E van KesterenJ Joosse
Sep 1, 1990·International Journal of Peptide and Protein Research·G MichelR Acher
Jan 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·S BurmanE Breslow
Jan 1, 1987·International Journal of Peptide and Protein Research·C H LiM M Oosthuizen
Oct 1, 1985·International Journal of Peptide and Protein Research·H S SaaymanW Oelofsen
May 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·M T ChauvetR Acher

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