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1bp3

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bp3 OCA], [http://www.ebi.ac.uk/pdbsum/1bp3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bp3 RCSB]</span>
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'''THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR COMPLEX'''
'''THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR COMPLEX'''
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[[Category: Ultsch, M.]]
[[Category: Ultsch, M.]]
[[Category: Vos, A M.De.]]
[[Category: Vos, A M.De.]]
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[[Category: hormone]]
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[[Category: Hormone]]
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[[Category: hormone/growth factor]]
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[[Category: Hormone/growth factor]]
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[[Category: receptor]]
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[[Category: Receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:47:27 2008''
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Revision as of 08:47, 2 May 2008

Template:STRUCTURE 1bp3

THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR COMPLEX


Overview

The human pituitary hormones, growth hormone (hGH) and prolactin (hPRL), regulate a large variety of physiological processes, among which are growth and differentiation of muscle, bone and cartilage cells, and lactation. These activities are initiated by hormone-receptor binding. The hGH and hPRL receptors (hGHR and hPRLR, respectively) are single-pass transmembrane receptors from class 1 of the haematopoietic receptor superfamily. This classification is based on sequence similarity in their extracellular domains, notably a highly conserved pentapeptide, the so-called 'WSXWS box', the function of which is controversial. All ligands in class 1 activate their respective receptors by clustering mechanisms. In the case of hGH, activation involves receptor homodimerization in a sequential process: the active ternary complex containing one ligand and two receptor molecules is formed by association of a receptor molecule to an intermediate 1:1 complex. hPRL does not bind to the hGH receptor, but hGH binds to both the hGHR and hPRLR, and mutagenesis studies have shown that the receptor-binding sites on hGH overlap. We present here the crystal structure of the 1:1 complex of hGH bound to the extracellular domain of the hPRLR. Comparisons with the hGH-hGHR complex reveal how hGH can bind to the two distinctly different receptor binding surfaces.

About this Structure

1BP3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The X-ray structure of a growth hormone-prolactin receptor complex., Somers W, Ultsch M, De Vos AM, Kossiakoff AA, Nature. 1994 Dec 1;372(6505):478-81. PMID:7984244 Page seeded by OCA on Fri May 2 11:47:27 2008

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