TY - JOUR
T1 - NMR Studies of Toxin III from the Sea Anemone Radianthus paumotensis and Comparison of Its Secondary Structure with Related Toxins
AU - Pease, Joseph H.B.
AU - Kumar, N. Vasant
AU - Schweitz, Hugues
AU - Kallenbach, Neville R.
AU - Wemmer, David E.
PY - 1989
Y1 - 1989
N2 - Nearly complete assignments of the proton nuclear magnetic resonance (NMR) spectrum of the polypeptide toxin III from the sea anemone Radianthus paumotensis (RP) are presented. The secondary structures of the related toxins RP II and RP III are described and are compared with each other and with another related toxin ATX la from Anemonia sulcata [Widmer, H., Wagner, G., Schweitz, H., Lazdunski, M., & Wüthrich, K. (1988) Eur. J. Biochem. 171, 177–192], All of these proteins contain a highly twisted four-strand antiparallel β-sheet core connected by loops of irregular structure. From the work done with AP-A from Anthopleura xanthogrammica [Gooley, P. R., & Norton, R. S. (1986) Biochemistry 25, 2349-2356], it is clear that this homologous toxin also has the same basic core. Some small differences are seen in the structures of these toxins, particularly in the position of the N-terminal residues that form one of the outside strands of the β-sheet. In addition, the R. paumotensis toxins are two residues longer, extending the third strand of sheet containing the C-terminal residues. A comparison of chemical shifts for assigned residues is also presented, in general supporting the similarity of structure among these proteins.
AB - Nearly complete assignments of the proton nuclear magnetic resonance (NMR) spectrum of the polypeptide toxin III from the sea anemone Radianthus paumotensis (RP) are presented. The secondary structures of the related toxins RP II and RP III are described and are compared with each other and with another related toxin ATX la from Anemonia sulcata [Widmer, H., Wagner, G., Schweitz, H., Lazdunski, M., & Wüthrich, K. (1988) Eur. J. Biochem. 171, 177–192], All of these proteins contain a highly twisted four-strand antiparallel β-sheet core connected by loops of irregular structure. From the work done with AP-A from Anthopleura xanthogrammica [Gooley, P. R., & Norton, R. S. (1986) Biochemistry 25, 2349-2356], it is clear that this homologous toxin also has the same basic core. Some small differences are seen in the structures of these toxins, particularly in the position of the N-terminal residues that form one of the outside strands of the β-sheet. In addition, the R. paumotensis toxins are two residues longer, extending the third strand of sheet containing the C-terminal residues. A comparison of chemical shifts for assigned residues is also presented, in general supporting the similarity of structure among these proteins.
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U2 - 10.1021/bi00431a034
DO - 10.1021/bi00431a034
M3 - Article
C2 - 2566327
AN - SCOPUS:0024595939
VL - 28
SP - 2199
EP - 2204
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 5
ER -