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1bp3
From Proteopedia
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| - | [[Image:1bp3.jpg|left|200px]] | + | [[Image:1bp3.jpg|left|200px]] |
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| - | '''THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR COMPLEX''' | + | {{Structure |
| + | |PDB= 1bp3 |SIZE=350|CAPTION= <scene name='initialview01'>1bp3</scene>, resolution 2.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BP3 is a [ | + | 1BP3 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BP3 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/7984244 7984244] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: receptor]] | [[Category: receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:13:57 2008'' |
Revision as of 08:14, 20 March 2008
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| , resolution 2.90Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE XRAY STRUCTURE OF A GROWTH HORMONE-PROLACTIN RECEPTOR COMPLEX
Contents |
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.
Disease
Known diseases associated with this structure: Growth hormone deficiency OMIM:[139250], Growth hormone deficiency, isolated, type IA OMIM:[139250], Growth hormone deficiency, isolated, type IB OMIM:[139250], Growth hormone deficiency, isolated, type II OMIM:[139250], Kowarski syndrome OMIM:[139250], Short stature, familial OMIM:[139250]
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 Thu Mar 20 10:13:57 2008
