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| | ==Prolactin Receptor (PRLR) Complexed with the Natural Hormone (PRL)== | | ==Prolactin Receptor (PRLR) Complexed with the Natural Hormone (PRL)== |
| - | <StructureSection load='3npz' size='340' side='right' caption='[[3npz]], [[Resolution|resolution]] 3.35Å' scene=''> | + | <StructureSection load='3npz' size='340' side='right'caption='[[3npz]], [[Resolution|resolution]] 3.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3npz]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NPZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NPZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3npz]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NPZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NPZ FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hCG_36753, PRL, RP3-404K8.1-001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Prlr ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3npz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3npz OCA], [http://pdbe.org/3npz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3npz RCSB], [http://www.ebi.ac.uk/pdbsum/3npz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3npz ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3npz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3npz OCA], [https://pdbe.org/3npz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3npz RCSB], [https://www.ebi.ac.uk/pdbsum/3npz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3npz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PRL_HUMAN PRL_HUMAN]] Prolactin acts primarily on the mammary gland by promoting lactation. [[http://www.uniprot.org/uniprot/PRLR_RAT PRLR_RAT]] This is a receptor for the anterior pituitary hormone prolactin. | + | [https://www.uniprot.org/uniprot/PRL_HUMAN PRL_HUMAN] Prolactin acts primarily on the mammary gland by promoting lactation. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| | *[[Prolactin|Prolactin]] | | *[[Prolactin|Prolactin]] |
| - | *[[Prolactin (Hebrew)|Prolactin (Hebrew)]] | |
| | *[[Prolactin receptor|Prolactin receptor]] | | *[[Prolactin receptor|Prolactin receptor]] |
| | == References == | | == References == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]] | + | [[Category: Large Structures]] |
| - | [[Category: Agthoven, J Van]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Broutin, I]] | + | [[Category: Broutin I]] |
| - | [[Category: England, P]] | + | [[Category: England P]] |
| - | [[Category: Goffin, V]] | + | [[Category: Goffin V]] |
| - | [[Category: Hormone]] | + | [[Category: Van Agthoven J]] |
| - | [[Category: Hormone-hormone receptor complex]]
| + | |
| - | [[Category: Hormone-receptor complex]]
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| - | [[Category: Protein protein complex]]
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| Structural highlights
Function
PRL_HUMAN Prolactin acts primarily on the mammary gland by promoting lactation.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The most promising approach to targeting the tumor-growth-promoting actions of prolactin (PRL) mediated by its autocrine/paracrine pathway has been the development of specific PRL receptor (PRLR) antagonists. However, the optimization of such antagonists requires a thorough understanding of the activation mechanism of PRLR. We have thus conducted a systematic X-ray crystallographic study in order to visualize the successive steps of PRLR activation by PRL. We report here the structure at 3.35 A resolution of the 1:2 complex between natural PRL and two PRLR chains (PRLR1 and PRLR2), corresponding to the final activated state of PRLR. Further than our previously published structure involving an affinity-matured PRL variant, this structure allowed to visualize for the first time the loop L5 spanning PRLR2 residues Thr133-Phe140, revealing its central implication for the three intermolecular interfaces of the complex. We equally succeeded in obtaining a comprehensive picture of the PRLR-PRLR dimerization interface, also called stem-stem interface. Site-directed mutagenesis was conducted to probe the energetic importance of stem-stem contacts highlighted by the structure. Surprisingly, in spite of significant structural differences between the PRL/PRLR(2) complex and the growth hormone/growth hormone receptor 2 complex, our mutational data suggest that hot-spot residues that stabilize the receptor dimerization interface are equivalent in the two complexes. This study provides a new overall picture of the structural features of PRLR involved in stabilizing its complex with PRL.
Structural Characterization of the Stem-Stem Dimerization Interface between Prolactin Receptor Chains Complexed with the Natural Hormone.,van Agthoven J, Zhang C, Tallet E, Raynal B, Hoos S, Baron B, England P, Goffin V, Broutin I J Mol Biol. 2010 Sep 25. PMID:20875426[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ van Agthoven J, Zhang C, Tallet E, Raynal B, Hoos S, Baron B, England P, Goffin V, Broutin I. Structural Characterization of the Stem-Stem Dimerization Interface between Prolactin Receptor Chains Complexed with the Natural Hormone. J Mol Biol. 2010 Sep 25. PMID:20875426 doi:10.1016/j.jmb.2010.09.036
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