13C nuclear magnetic resonance studies of the interactions of bovine neurophysins with (1‐hemi‐[1‐13C]cystine)oxytocin and (1‐hemi‐[1‐13C]cystine, 8‐arginine)vasopressin

Blumenstein, Michael; Hruby, Victor J.; Yamamoto, Diane M.; Yang, Young C. S.

doi:10.1016/0014-5793(77)80551-6

Cited by 16 publications

(1 citation statement)

References 20 publications

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“…The importance of the peptide a-amino group of oxytocin for binding to neurophysin was first recognized by the failure of deaminooxytocin to bind to neurophysin (Stouffer et al, 1963). It was also shown that its pK is elevated by at least 5 pH units in the complex relative to the unliganded state, consistent with the formation of a salt bridge in a nonpolar environment (Blumenstein et al, 1977). In our bound conformation, the a-amino group is sticking outwards and forms no interactions with the rest of the peptide.…”

Section: A) (A(a)/(aa)) Angle (A) ( a ( A ) / ( A A ) ) Angle (A) (A(supporting

confidence: 61%

Transfer nuclear Overhauser effect study of the conformation of oxytocin bound to bovine neurophysin I

Lippens

Belle²,

Wodak³

et al. 1993

Biochemistry

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This study reports the structure of the peptide hormone oxytocin bound to its carrier protein, neurophysin I, obtained by nuclear magnetic resonance techniques. At the pH value of 2.1 in our experiments, the ligand is in fast exchange with its carrier protein, allowing the use of transfer-NOE methods. The number of distance constraints for the peptide being limited, considerable attention has been paid to an accurate distance determination. The resulting accurate distance limits were used as input for a distance geometry calculation followed by a restrained molecular dynamics run. Convergence to a well-defined family of structures for oxytocin in its bound state was reached. Both the backbone and the side-chain conformations differ between the bound form and the crystal structure of free oxytocin [Wood, S. P., et al. (1986) Science 232, 633]. These differences, as well as other structural features of the bound form, are discussed in terms of interactions made with the carrier protein. Transfer-NOE experiments at low peptide protein ratios provide direct experimental evidence for contacts between the oxytocin Tyr2 residue and an aromatic residue of neurophysin. The resonance assignments of the aromatic groups [Whittaker, B. A., et al. (1985) Biochemistry 24, 2782] together with the recently published X-ray structure of the neurophysin II protein complexed with a dipeptide [Chen et al. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 4240] allow us to assign the aromatic signal on the protein to the neurophysin Phe22 residue.

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Section: A) (A(a)/(aa)) Angle (A) ( a ( A ) / ( A A ) ) Angle (A) (A(supporting

confidence: 61%

Transfer nuclear Overhauser effect study of the conformation of oxytocin bound to bovine neurophysin I

Lippens

Belle²,

Wodak³

et al. 1993

Biochemistry

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Molecular, Thermodynamic, and Biological Aspects of Recognition and Function in Neurophysin‐Hormone Systems: A Model System for the Analysis of Protein–Peptide Interactions

Breslow

Burman

1990

Advances in Enzymology - And Related Areas of Molecular Biology

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Synthesis of S‐benzyl‐DL‐[1‐¹³C]cysteine and its incorporation into oxytocin and [8‐arginlne]vasopressin and related compounds by total synthesis. Separation of diastekeoisomers by partition chromatography and HPLC

Hruby¹,

Viswanatha²,

Yang³

1980

Labelled Comp Radiopharmac

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¹³C nuclear magnetic resonance studies of the interactions of bovine neurophysins with (1‐hemi‐[1‐¹³C]cystine)oxytocin and (1‐hemi‐[1‐¹³C]cystine, 8‐arginine)vasopressin

Cited by 16 publications

References 20 publications

Transfer nuclear Overhauser effect study of the conformation of oxytocin bound to bovine neurophysin I

Transfer nuclear Overhauser effect study of the conformation of oxytocin bound to bovine neurophysin I

Molecular, Thermodynamic, and Biological Aspects of Recognition and Function in Neurophysin‐Hormone Systems: A Model System for the Analysis of Protein–Peptide Interactions

Synthesis of S‐benzyl‐DL‐[1‐¹³C]cysteine and its incorporation into oxytocin and [8‐arginlne]vasopressin and related compounds by total synthesis. Separation of diastekeoisomers by partition chromatography and HPLC

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13C nuclear magnetic resonance studies of the interactions of bovine neurophysins with (1‐hemi‐[1‐13C]cystine)oxytocin and (1‐hemi‐[1‐13C]cystine, 8‐arginine)vasopressin

Cited by 16 publications

References 20 publications

Transfer nuclear Overhauser effect study of the conformation of oxytocin bound to bovine neurophysin I

Transfer nuclear Overhauser effect study of the conformation of oxytocin bound to bovine neurophysin I

Molecular, Thermodynamic, and Biological Aspects of Recognition and Function in Neurophysin‐Hormone Systems: A Model System for the Analysis of Protein–Peptide Interactions

Synthesis of S‐benzyl‐DL‐[1‐13C]cysteine and its incorporation into oxytocin and [8‐arginlne]vasopressin and related compounds by total synthesis. Separation of diastekeoisomers by partition chromatography and HPLC

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¹³C nuclear magnetic resonance studies of the interactions of bovine neurophysins with (1‐hemi‐[1‐¹³C]cystine)oxytocin and (1‐hemi‐[1‐¹³C]cystine, 8‐arginine)vasopressin

Synthesis of S‐benzyl‐DL‐[1‐¹³C]cysteine and its incorporation into oxytocin and [8‐arginlne]vasopressin and related compounds by total synthesis. Separation of diastekeoisomers by partition chromatography and HPLC