Crystallization of ovine placental lactogen in a 1:2 complex with the extracellular domain of the rat prolactin receptor
Autor: | Anthony A. Kossiakoff, Y. Sandowski, E. Sakal, Arieh Gertler, P.A. Elkins, H.W. Christinger, A.M. de Vos |
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Rok vydání: | 1999 |
Předmět: |
endocrine system
medicine.medical_specialty Macromolecular Substances Protein Conformation Receptors Prolactin Recombinant Fusion Proteins Crystallography X-Ray law.invention Prolactin cell Structural Biology law Internal medicine medicine Extracellular Endocrine system Animals Crystallization Placental lactogen Receptor Sheep Chemistry Prolactin receptor General Medicine Placental Lactogen Prolactin Rats Endocrinology hormones hormone substitutes and hormone antagonists |
Zdroj: | Acta crystallographica. Section D, Biological crystallography. 54(Pt 6 Pt 2) |
ISSN: | 0907-4449 |
Popis: | 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. |
Databáze: | OpenAIRE |
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