1f6f
From Proteopedia
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| , resolution 2.3Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE TERNARY COMPLEX BETWEEN OVINE PLACENTAL LACTOGEN AND THE EXTRACELLULAR DOMAIN OF THE RAT PROLACTIN RECEPTOR
Overview
The structure of the ternary complex between ovine placental lactogen (oPL) and the extracellular domain (ECD) of the rat prolactin receptor (rPRLR) reveals that two rPRLR ECDs bind to opposite sides of oPL with pseudo two-fold symmetry. The two oPL receptor binding sites differ significantly in their topography and electrostatic character. These binding interfaces also involve different hydrogen bonding and hydrophobic packing patterns compared to the structurally related human growth hormone (hGH)-receptor complexes. Additionally, the receptor-receptor interactions are different from those of the hGH-receptor complex. The conformational adaptability of prolactin and growth hormone receptors is evidenced by the changes in local conformations of the receptor binding loops and more global changes induced by shifts in the angular relationships between the N- and C-terminal domains, which allow the receptor to bind to the two topographically distinct sites of oPL.
About this Structure
1F6F is a Protein complex structure of sequences from Ovis aries and Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Ternary complex between placental lactogen and the extracellular domain of the prolactin receptor., Elkins PA, Christinger HW, Sandowski Y, Sakal E, Gertler A, de Vos AM, Kossiakoff AA, Nat Struct Biol. 2000 Sep;7(9):808-15. PMID:10966654
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