1F6F

CRYSTAL STRUCTURE OF THE TERNARY COMPLEX BETWEEN OVINE PLACENTAL LACTOGEN AND THE EXTRACELLULAR DOMAIN OF THE RAT PROLACTIN RECEPTOR

Summary for 1F6F

• Entry DOI: 10.2210/pdb1f6f/pdb
• Descriptor: PLACENTAL LACTOGEN, PROLACTIN RECEPTOR (3 entities in total)
• Functional Keywords: 4-helical bundle, alpha helical bundle, ternary complex, fn iii domains, beta sheet domains, cytokine-receptor complex, hormone-growth factor-hormone receptor complex, hormone/growth factor/hormone receptor
• Biological source: Ovis aries (sheep); More
• Cellular location: Secreted: P16038; Membrane; Single-pass type I membrane protein: P05710
• Total number of polymer chains: 3
• Total formula weight: 71770.63

Authors

Elkins, P.A.,Christinger, H.W.,Sandowski, Y.,Sakal, E.,Gertler, A.,De Vos, A.M.,Kossiakoff, A.A. (deposition date: 2000-06-21, release date: 2000-07-04, Last modification date: 2024-10-30)

Primary citation

Elkins, P.A.,Christinger, H.W.,Sandowski, Y.,Sakal, E.,Gertler, A.,de Vos, A.M.,Kossiakoff, A.A.
Ternary complex between placental lactogen and the extracellular domain of the prolactin receptor.
Nat.Struct.Biol., 7:808-815, 2000

PubMed Abstract: 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.

PubMed: 10966654
DOI: 10.1038/79047

Experimental method

X-RAY DIFFRACTION (2.3 Å)