Crystallization of ovine placental lactogen in a 1:2 complex with the extracellular domain of the rat prolactin receptor

Hans W. Christinger; Patricia A. Elkins; Yael Sandowski; Edna Sakal; Arieh Gertler; Anthony A. Kossiakoff; Abraham M. De Vos

doi:10.1107/s0907444998005794

Crystallization of ovine placental lactogen in a 1:2 complex with the extracellular domain of the rat prolactin receptor

Hans W. Christinger, Patricia A. Elkins, Yael Sandowski, Edna Sakal, Arieh Gertler, Anthony A. Kossiakoff, Abraham M. De Vos^*

^*Corresponding author for this work

Institute of Biochemistry, Food Science and Nutrition

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

Abstract

Growth hormone and prolactin control somato-lactogenic biology. While high-resolution crystal structures have been determined for receptor complexes of human growth hormone, no such information exists for prolactin. A stable 1:2 complex was formed between ovine placental lactogen, a close prolactin homologue, and two copies of the extracellular portion of the rat prolactin receptor. Using synchrotron radiation, native data have been collected to 2.3 Å. Crystals contain one complex per asymmetric unit. The crystal structure of this complex will shed light on the structural reasons for cross-reactivity and specificity among the endocrine hormones, placental lactogen, prolactin and growth hormone.

Original language	English
Pages (from-to)	1408-1411
Number of pages	4
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	54
Issue number	6 PART II
DOIs	https://doi.org/10.1107/s0907444998005794
State	Published - 1998

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abstract = "Growth hormone and prolactin control somato-lactogenic biology. While high-resolution crystal structures have been determined for receptor complexes of human growth hormone, no such information exists for prolactin. A stable 1:2 complex was formed between ovine placental lactogen, a close prolactin homologue, and two copies of the extracellular portion of the rat prolactin receptor. Using synchrotron radiation, native data have been collected to 2.3 {\AA}. Crystals contain one complex per asymmetric unit. The crystal structure of this complex will shed light on the structural reasons for cross-reactivity and specificity among the endocrine hormones, placental lactogen, prolactin and growth hormone.",

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AU - Christinger, Hans W.

AU - Elkins, Patricia A.

AU - Sandowski, Yael

AU - Sakal, Edna

AU - Gertler, Arieh

AU - Kossiakoff, Anthony A.

AU - De Vos, Abraham M.

PY - 1998

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AB - Growth hormone and prolactin control somato-lactogenic biology. While high-resolution crystal structures have been determined for receptor complexes of human growth hormone, no such information exists for prolactin. A stable 1:2 complex was formed between ovine placental lactogen, a close prolactin homologue, and two copies of the extracellular portion of the rat prolactin receptor. Using synchrotron radiation, native data have been collected to 2.3 Å. Crystals contain one complex per asymmetric unit. The crystal structure of this complex will shed light on the structural reasons for cross-reactivity and specificity among the endocrine hormones, placental lactogen, prolactin and growth hormone.

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Crystallization of ovine placental lactogen in a 1:2 complex with the extracellular domain of the rat prolactin receptor

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