1an3

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THE RABBIT PROLACTIN HORMONE COMPLEXED WITH THE EXTRACELLULAR DOMAIN OF ITS RECEPTOR, THEORETICAL MODEL

spinqualitylabelsall models 1an3 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum, ProSAT Publication Abstract from PubMed The pituitary hormone prolactin (prl) is implicated in a number of biological functions, especially lactation, which is mediated through specific lactogenic receptors (PrlR). Human growth hormone (hGH) is also a pituitary hormone responsible for linear growth. While the growth hormone receptor (hGHR) binds only hGH, hPrlR can interact with both hGH and hPrl. Using structural information from the human growth hormone (hGH)/receptor (hGHR) complex, we modeled by homology a complex between rabbit prolactin hormone (rbPrl) and its receptor (rbPrlR). While the somatogenic hormone/somatogenic receptor (hGH/hGHR) and somatogenic hormone/lactogenic receptor (hGH/hPrlR) interactions are now known and well studied, here we propose a model for the interaction of the lactogenic hormone with its receptor (rbPrl/rbPrlR), and compare these three kinds of ligand/receptor interaction. We identified residues contributing to the active site and tested the potential dimerization of the receptor. Biochemical studies and information deduced from the modeled complex do not exclude a homodimeric form but point to a functional heterodimeric complex. Homology modeling of rabbit prolactin hormone complexed with its receptor.,Halaby D, Thoreau E, Djiane J, Mornon JP Proteins. 1997 Mar;27(3):459-68. PMID:9094747 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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