The conformation of deamino-oxytocin: X-ray analysis of the 'dry' and 'wet' forms.

J. Husain, T. L. Blundell, S. Cooper, J. E. Pitts, I. J. Tickle, S. P. Wood, Victor J Hruby, A. Buku, A. J. Fischman, H. R. Wyssbrod

Research output: Contribution to journalArticle

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Abstract

Two crystal structures of (1 beta-mercaptopropionic acid) deamino-oxytocin are reported. The 'dry form' in space group C2 has cell dimensions a = 27.08 +/- 0.03, b = 9.06 +/- 0.01, c = 22.98 +/- 0.02 A, beta = 102.06 +/- 0.03 with one deamino-oxytocin and six water molecules per asymmetric unit. The 'wet form' in space group P2(1) has cell dimensions a = 27.27 +/- 0.02, b = 9.04 +/- 0.01, c = 23.04 +/- 0.02 A, beta = 102.24 +/- 0.02, with two deamino-oxytocin and 13 water molecules per asymmetric unit. A local twofold parallel to the monoclinic axis gives a pseudo C2 packing. Initial phases of the 'dry form' were calculated by the heavy-atom method from the isomorphous and anomalous difference Pattersons and anomalous difference Fouier synthesis. The structure was refined by using restrained least-squares at 1.2 A resolution to a crystallographic R = 0.10. The molecular replacement method yielded the P2(1) structure that was refined with geometric restraints to R less than 0.09, by using all data to 1.09 A resolution. Deamino-oxytocin consists of a cyclic tocin ring formed by six amino acids, closed by a disulphide bridge, S1-S6, and held by two trans-annular hydrogen bonds N2-O5 and N5-O2 with a type II turn at residues 3 and 4. A flexible tripeptide tail has a loosely hydrogen-bonded type I beta-turn between N9 and O6. The sulphur of cysteine at position 1 is disordered in all the molecules leading to alternative hands of disulphide. The conformational flexibility of Ile 3, Asn 5, Pro 7 side chains and the disulphide bridge is consistent with previous models of oxytocin in which flexibility is necessary for biological activity.

Original languageEnglish (US)
Pages (from-to)625-654
Number of pages30
JournalPhilosophical transactions of the Royal Society of London. Series B: Biological sciences
Volume327
Issue number1243
StatePublished - Apr 27 1990
Externally publishedYes

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oxytocin
X ray analysis
Oxytocin
X-ray spectroscopy
Conformations
X-radiation
X-Rays
hydrogen
sulfides
Disulfides
crystal structure
amino acid
replacement
sulfur
Molecules
Hydrogen
water
acid
S 6
tripeptides

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)

Cite this

Husain, J., Blundell, T. L., Cooper, S., Pitts, J. E., Tickle, I. J., Wood, S. P., ... Wyssbrod, H. R. (1990). The conformation of deamino-oxytocin: X-ray analysis of the 'dry' and 'wet' forms. Philosophical transactions of the Royal Society of London. Series B: Biological sciences, 327(1243), 625-654.

The conformation of deamino-oxytocin : X-ray analysis of the 'dry' and 'wet' forms. / Husain, J.; Blundell, T. L.; Cooper, S.; Pitts, J. E.; Tickle, I. J.; Wood, S. P.; Hruby, Victor J; Buku, A.; Fischman, A. J.; Wyssbrod, H. R.

In: Philosophical transactions of the Royal Society of London. Series B: Biological sciences, Vol. 327, No. 1243, 27.04.1990, p. 625-654.

Research output: Contribution to journalArticle

Husain, J, Blundell, TL, Cooper, S, Pitts, JE, Tickle, IJ, Wood, SP, Hruby, VJ, Buku, A, Fischman, AJ & Wyssbrod, HR 1990, 'The conformation of deamino-oxytocin: X-ray analysis of the 'dry' and 'wet' forms.', Philosophical transactions of the Royal Society of London. Series B: Biological sciences, vol. 327, no. 1243, pp. 625-654.
Husain, J. ; Blundell, T. L. ; Cooper, S. ; Pitts, J. E. ; Tickle, I. J. ; Wood, S. P. ; Hruby, Victor J ; Buku, A. ; Fischman, A. J. ; Wyssbrod, H. R. / The conformation of deamino-oxytocin : X-ray analysis of the 'dry' and 'wet' forms. In: Philosophical transactions of the Royal Society of London. Series B: Biological sciences. 1990 ; Vol. 327, No. 1243. pp. 625-654.
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abstract = "Two crystal structures of (1 beta-mercaptopropionic acid) deamino-oxytocin are reported. The 'dry form' in space group C2 has cell dimensions a = 27.08 +/- 0.03, b = 9.06 +/- 0.01, c = 22.98 +/- 0.02 A, beta = 102.06 +/- 0.03 with one deamino-oxytocin and six water molecules per asymmetric unit. The 'wet form' in space group P2(1) has cell dimensions a = 27.27 +/- 0.02, b = 9.04 +/- 0.01, c = 23.04 +/- 0.02 A, beta = 102.24 +/- 0.02, with two deamino-oxytocin and 13 water molecules per asymmetric unit. A local twofold parallel to the monoclinic axis gives a pseudo C2 packing. Initial phases of the 'dry form' were calculated by the heavy-atom method from the isomorphous and anomalous difference Pattersons and anomalous difference Fouier synthesis. The structure was refined by using restrained least-squares at 1.2 A resolution to a crystallographic R = 0.10. The molecular replacement method yielded the P2(1) structure that was refined with geometric restraints to R less than 0.09, by using all data to 1.09 A resolution. Deamino-oxytocin consists of a cyclic tocin ring formed by six amino acids, closed by a disulphide bridge, S1-S6, and held by two trans-annular hydrogen bonds N2-O5 and N5-O2 with a type II turn at residues 3 and 4. A flexible tripeptide tail has a loosely hydrogen-bonded type I beta-turn between N9 and O6. The sulphur of cysteine at position 1 is disordered in all the molecules leading to alternative hands of disulphide. The conformational flexibility of Ile 3, Asn 5, Pro 7 side chains and the disulphide bridge is consistent with previous models of oxytocin in which flexibility is necessary for biological activity.",
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AU - Cooper, S.

AU - Pitts, J. E.

AU - Tickle, I. J.

AU - Wood, S. P.

AU - Hruby, Victor J

AU - Buku, A.

AU - Fischman, A. J.

AU - Wyssbrod, H. R.

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N2 - Two crystal structures of (1 beta-mercaptopropionic acid) deamino-oxytocin are reported. The 'dry form' in space group C2 has cell dimensions a = 27.08 +/- 0.03, b = 9.06 +/- 0.01, c = 22.98 +/- 0.02 A, beta = 102.06 +/- 0.03 with one deamino-oxytocin and six water molecules per asymmetric unit. The 'wet form' in space group P2(1) has cell dimensions a = 27.27 +/- 0.02, b = 9.04 +/- 0.01, c = 23.04 +/- 0.02 A, beta = 102.24 +/- 0.02, with two deamino-oxytocin and 13 water molecules per asymmetric unit. A local twofold parallel to the monoclinic axis gives a pseudo C2 packing. Initial phases of the 'dry form' were calculated by the heavy-atom method from the isomorphous and anomalous difference Pattersons and anomalous difference Fouier synthesis. The structure was refined by using restrained least-squares at 1.2 A resolution to a crystallographic R = 0.10. The molecular replacement method yielded the P2(1) structure that was refined with geometric restraints to R less than 0.09, by using all data to 1.09 A resolution. Deamino-oxytocin consists of a cyclic tocin ring formed by six amino acids, closed by a disulphide bridge, S1-S6, and held by two trans-annular hydrogen bonds N2-O5 and N5-O2 with a type II turn at residues 3 and 4. A flexible tripeptide tail has a loosely hydrogen-bonded type I beta-turn between N9 and O6. The sulphur of cysteine at position 1 is disordered in all the molecules leading to alternative hands of disulphide. The conformational flexibility of Ile 3, Asn 5, Pro 7 side chains and the disulphide bridge is consistent with previous models of oxytocin in which flexibility is necessary for biological activity.

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