1an3: Difference between revisions

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 {{Theoretical_model}}
-{{Seed}}
-[[Image:1an3.png|left|200px]]
-<!--
+==THE RABBIT PROLACTIN HORMONE COMPLEXED WITH THE EXTRACELLULAR DOMAIN OF ITS RECEPTOR, THEORETICAL MODEL==
-The line below this paragraph, containing "STRUCTURE_1an3", creates the "Structure Box" on the page.
+<StructureSection load='1an3' size='340' side='right'caption='[[1an3]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AN3 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=1an3 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1an3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1an3 ProSAT]</span></td></tr>
--->
+</table>
-{{STRUCTURE_1an3|  PDB=1an3  |  SCENE=  }}
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The pituitary hormone prolactin (prl) is implicated in a number of biological functions, especially lactation, which is mediated through specific lactogenic receptors (PrlR). Human growth hormone (hGH) is also a pituitary hormone responsible for linear growth. While the growth hormone receptor (hGHR) binds only hGH, hPrlR can interact with both hGH and hPrl. Using structural information from the human growth hormone (hGH)/receptor (hGHR) complex, we modeled by homology a complex between rabbit prolactin hormone (rbPrl) and its receptor (rbPrlR). While the somatogenic hormone/somatogenic receptor (hGH/hGHR) and somatogenic hormone/lactogenic receptor (hGH/hPrlR) interactions are now known and well studied, here we propose a model for the interaction of the lactogenic hormone with its receptor (rbPrl/rbPrlR), and compare these three kinds of ligand/receptor interaction. We identified residues contributing to the active site and tested the potential dimerization of the receptor. Biochemical studies and information deduced from the modeled complex do not exclude a homodimeric form but point to a functional heterodimeric complex.
-===THE RABBIT PROLACTIN HORMONE COMPLEXED WITH THE EXTRACELLULAR DOMAIN OF ITS RECEPTOR, THEORETICAL MODEL===
+Homology modeling of rabbit prolactin hormone complexed with its receptor.,Halaby D, Thoreau E, Djiane J, Mornon JP Proteins. 1997 Mar;27(3):459-68. PMID:9094747<ref>PMID:9094747</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_9094747}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1an3" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 9094747 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_9094747}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN3 OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:9094747</ref><references group="xtra"/>
 [[Category: Halaby, D]]
 [[Category: Mornon, J P]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 08:40:22 2010''