The Rowland Institute at Harvard

Biophysical Chem Lab


Jeff Hoch
Alan Stern


Human Prolactin
NMR Data Processing
  Structure Calculations

Group Alumni

Peter Connolly
Claudio Chuaqui
Eric LaRosa
Kuo-Bin Li
George Maalouf
John Osterhout

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Human Prolactin

Prolactin is a 199-residue member of the hematopoeitic cytokine family, named for its role in stimulating lactation during pregnancy. It is also involved in a number of other signaling pathways, including immune response. It is homologous to growth hormone, which is the most extensively studied member of the family. The structure of prolactin is of considerable interest because it binds only to its receptor, whereas growth hormone binds both to its own receptor and to the prolactin receptor. It has an unusual up-up-down-down four-helix bundle topology. In collaboration with Prof. Joseph Martial's group at the Universite de Liege we are determining the structure by heteronuclear multidimensional NMR. The folding and unfolding properties of prolactin have proven to be unusual, and potentially useful as a model system for studies on protein folding and stability.

Depicted below is the structure of growth hormone bound to two copies of the extracellular domain of the somatogenic receptor, as determined by A. Kossiakoff and colleagues at Genentech.

Copyright © 2002 The Rowland Institute at Harvard.

Last modified Thursday, October 09, 2003.