PDBsum entry 1f6f

Hormone/growth factor/hormone receptor

PDB id: 1f6f

Contents

Protein chains

183 a.a. *

195 a.a. *

169 a.a. *

Waters ×120

* Residue conservation analysis

PDB id:

1f6f

Name:

Hormone/growth factor/hormone receptor

Title:

Crystal structure of the ternary complex between ovine placental lactogen and the extracellular domain of the rat prolactin receptor

Structure:

Placental lactogen. Chain: a. Engineered: yes. Prolactin receptor. Chain: b, c. Fragment: extracellular domain. N-terminal fibronectin type iii domains. Engineered: yes

Source:

Ovis aries. Sheep. Organism_taxid: 9940. Expressed in: escherichia coli. Expression_system_taxid: 562. Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: liver.

Biol. unit:

Hexamer (from PQS)

Resolution:

2.30Å R-factor: 0.225 R-free: 0.287

Authors:

P.A.Elkins,H.W.Christinger,Y.Sandowski,E.Sakal,A.Gertler,A.M.De Vos, A.A.Kossiakoff

Key ref:

P.A.Elkins et al. (2000). Ternary complex between placental lactogen and the extracellular domain of the prolactin receptor. Nat Struct Biol, 7, 808-815. PubMed id: 10966654 DOI: 10.1038/79047

Date:

21-Jun-00 Release date: 04-Jul-00

Protein chain

P16038  (CSH_SHEEP) -  Chorionic somatomammotropin hormone from Ovis aries

Seq: 236 a.a.

Struc: 183 a.a.

Protein chain

P05710  (PRLR_RAT) -  Prolactin receptor from Rattus norvegicus

Seq: 610 a.a.

Struc: 195 a.a.

Protein chain

P05710  (PRLR_RAT) -  Prolactin receptor from Rattus norvegicus

Seq: 610 a.a.

Struc: 169 a.a.

DOI no: 10.1038/79047

Nat Struct Biol 7:808-815 (2000)

PubMed id: 10966654

Ternary complex between placental lactogen and the extracellular domain of the prolactin receptor.

P.A.Elkins, H.W.Christinger, Y.Sandowski, E.Sakal, A.Gertler, A.M.de Vos, A.A.Kossiakoff.

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.

Selected figure(s)

Figure 1.
Figure 1. The oPL -rPRLR[2] ternary complex. The binding loops on R1 and R2 are numbered. Loops L1 -L3 are in the N-terminal domain of the receptor, L4 is in the linker region between the domains and L5 and L6 are in the C-terminal domain. In the R2 C-terminal domain, L5 and L6 are disordered. The -sheet cores of the domains of R1 and R2 superimpose with an r.m.s. deviation for the N-terminal domain of 0.8 Å for 53 C atoms; for the C-terminal domain the r.m.s. deviation is 0.5 Å for 63 C atoms.

Figure 2.
Figure 2. Ribbon diagram of oPL (left) and hGH (right). Helices 1 -4 are labeled on the oPL molecule, and the crossover loop between helices 1 and 2 and the mini-helix are labeled on the hGH molecule. The N-terminal extension on oPL is shown in yellow. In the oPL model, residues 46 -47, 96 -100 and 190 -191 are omitted due to disorder.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2000, 7, 808-815) copyright 2000.

Figures were selected by an automated process.