PROSITE documentation PDOC01050 [for PROSITE entry PS01352]

Long hematopoietin receptor, single chain family signature





Description

A number of receptors for lymphokines, hematopoietic growth factors and growth hormone-related molecules have been found to share a common binding domain. These receptors are designated as hematopoietin receptors [1,2] and the corresponding ligands as hematopoietins. Further, hematopoietins have been subdivided into two major structural groups: Large/long and small/short hematopoietins.

Several receptor chains for large hematopoietins are structurally related such that their extracellular parts strictly contain the 200 amino-acids hematopoietin domain, duplicated in the thrombopoietin receptor and in avian prolactin receptors. This subgroup of receptor chains contains:

  • Growth hormone receptor (GHR).
  • Prolactin receptor (PRLR).
  • Erythropoietin receptor (EPOR).
  • Thrombopoietin receptor (TPOR).

A schematic representation of the structure of these receptors is shown below:

 +----------------------------------------xxxxxxx-------------------------+
 | C C       C  C  Extracellular          XXXXXXX       Cytoplasmic       |
 +-|-|-------|--|-------------------------xxxxxxx-------------------------+
   | |       |  |                      Transmembrane
   +-+       +--+

These receptor chains are single components of receptors that homodimerize upon binding of the cognate cytokine, following the structural model described for the growth hormone-receptor complex [3].

We have used one pattern to detect this family. The motif is located in the carboxy-terminal part of the 200 amino acid hematopoietin domain.

Expert(s) to contact by email:

Boulay J.-L.

Last update:

December 2001 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

HEMATOPO_REC_L_F1, PS01352; Long hematopoietin receptor, single chain family signature  (PATTERN)


References

1AuthorsBoulay J.-L., Paul W.E.
TitleHematopoietin sub-family classification based on size, gene organization and sequence homology.
SourceCurr. Biol. 3:573-581(1993).
PubMed ID15335670

2AuthorsSprang S.R., Bazan J.F.
SourceCurrent Opin. Struct. Biol. 3:815-827(1993).

3Authorsde Vos A.M., Ultsch M., Kossiakoff A.A.
TitleHuman growth hormone and extracellular domain of its receptor: crystal structure of the complex.
SourceScience 255:306-312(1992).
PubMed ID1549776



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)