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Crystal structure of the neurophysin—oxytocin complex

Nature Structural Biology volume 3, pages 163–169 (1996)Cite this article

Abstract

The first crystal structure of the pituitary hormone oxytocin complexed with its carrier protein neurophysin has been determined and refined to 3.0 Å resolution. The hormone-binding site is located at the end of a 310-helix and involves residues from both domains of each monomer. Hormone residues Tyr 2, which is buried deep in the binding pocket, and Cys 1 have been confirmed as the key residues involved in neurophysin-hormone recognition. We have compared the bound oxytocin observed in the neurophysin–oxytocin complex, the X-ray structures of unbound oxytocin analogues and the NMR-derived structure for bound oxytocin. We find that while our structure is in agreement with the previous crystallographic findings, it differs from the NMR result with regard to how Tyr 2 of the hormone is recognized by neurophysin.

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Author information

Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University of Georgia Athens, Georgia, 30602, USA

    John P. Rose, Chia-Kuei Wu & Bi-Cheng Wang

  2. Department of Crystallography, University of Pittsburgh, Pittsburgh, Pennsylvania, 15260, USA

    Chia-Kuei Wu & Chwan-Deng Hsiao

  3. Institute of Molecular Biology, Academia Sinica, Taipei, Taiwan, 11529, ROC

    Chwan-Deng Hsiao

  4. Department of Biochemistry, Cornell University Medical College, New York, New York, 10021, USA

    Esther Breslow

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Rose, J., Wu, CK., Hsiao, CD. et al. Crystal structure of the neurophysin—oxytocin complex. Nat Struct Mol Biol 3, 163–169 (1996). https://doi.org/10.1038/nsb0296-163

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