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1rw5

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(New page: 200px<br /> <applet load="1rw5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rw5" /> '''Solution structure of human prolactin'''<br...)
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[[Image:1rw5.gif|left|200px]]<br />
 
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<applet load="1rw5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rw5" />
 
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'''Solution structure of human prolactin'''<br />
 
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==Overview==
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==Solution structure of human prolactin==
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We report the solution structure of human prolactin determined by NMR, spectroscopy. Our result is a significant improvement over a previous, structure in terms of number and distribution of distance restraints, regularity of secondary structure, and potential energy. More, significantly, the structure is sufficiently different that it leads to, different conclusions regarding the mechanism of receptor activation and, initiation of signal transduction. Here, we compare the structure of, unbound prolactin to structures of both the homologue ovine placental, lactogen and growth hormone. The structures of unbound and receptor bound, prolactin/placental lactogen are similar and no noteworthy structural, changes occur upon receptor binding. The observation of enhanced binding, at the second receptor site when the first site is occupied has been, widely interpreted to indicate conformational change induced by binding, the first receptor. However, our results indicate that this enhanced, binding at the second site could be due to receptor-receptor interactions, or some other free energy sources rather than conformational change in the, hormone. Titration of human prolactin with the extracellular domain of the, human prolactin receptor was followed by NMR, gel filtration and, electrophoresis. Both binary and ternary hormone-receptor complexes are, clearly detectable by gel filtration and electrophoresis. The binary, complex is not observable by NMR, possibly due to a dynamic equilibrium in, intermediate exchange within the complex. The ternary complex of one, hormone molecule bound to two receptor molecules is on the contrary, readily detectable by NMR. This is in stark contrast to the widely held, view that the ternary prolactin-receptor complex is only transiently, formed. Thus, our results lead to improved understanding of the, prolactin-prolactin receptor interaction.
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<StructureSection load='1rw5' size='340' side='right'caption='[[1rw5]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rw5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RW5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RW5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rw5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rw5 OCA], [https://pdbe.org/1rw5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rw5 RCSB], [https://www.ebi.ac.uk/pdbsum/1rw5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rw5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRL_HUMAN PRL_HUMAN] Prolactin acts primarily on the mammary gland by promoting lactation.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rw/1rw5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rw5 ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known diseases associated with this structure: Colorectal cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604584 604584]], Hepatocellular cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=604584 604584]]
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*[[Prolactin|Prolactin]]
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__TOC__
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==About this Structure==
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</StructureSection>
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1RW5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RW5 OCA].
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==Reference==
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Solution structure of human prolactin., Teilum K, Hoch JC, Goffin V, Kinet S, Martial JA, Kragelund BB, J Mol Biol. 2005 Aug 26;351(4):810-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16045928 16045928]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hoch, J.]]
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[[Category: Hoch J]]
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[[Category: Kragelund, B.B.]]
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[[Category: Kragelund BB]]
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[[Category: Martial, J.A.]]
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[[Category: Martial JA]]
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[[Category: Teilum, K.]]
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[[Category: Teilum K]]
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[[Category: cytokine]]
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[[Category: four helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:07:27 2007''
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Current revision

Solution structure of human prolactin

PDB ID 1rw5

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