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Article
Nature Structural Biology  3, 163 - 169 (1996)
doi:10.1038/nsb0296-163

Crystal structure of the neurophysin—oxytocin complex

John P. Rose1, Chia-Kuei Wu1, 2, Chwan-Deng Hsiao2, 3, Esther Breslow4 & Bi-Cheng Wang1

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

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

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

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

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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