3ncb: Difference between revisions

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-{{Seed}}
-[[Image:3ncb.png|left|200px]]
-<!--
+==A mutant human Prolactin receptor antagonist H180A in complex with the extracellular domain of the human prolactin receptor==
-The line below this paragraph, containing "STRUCTURE_3ncb", creates the "Structure Box" on the page.
+<StructureSection load='3ncb' size='340' side='right'caption='[[3ncb]], [[Resolution|resolution]] 2.10&Aring;' 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'>[[3ncb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NCB FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-{{STRUCTURE_3ncb|  PDB=3ncb  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ncb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ncb OCA], [https://pdbe.org/3ncb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ncb RCSB], [https://www.ebi.ac.uk/pdbsum/3ncb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ncb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PRL_HUMAN PRL_HUMAN] Prolactin acts primarily on the mammary gland by promoting lactation.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nc/3ncb_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=3ncb ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Human prolactin (hPRL), a member of the family of hematopoietic cytokines, functions as both an endocrine hormone and autocrine/paracrine growth factor. We have previously demonstrated that recognition of the hPRL receptor (hPRLr) depends strongly on solution acidity over the physiologic range from pH 6 &amp;- 8. The hPRL-receptor binding interface contains four histidines, whose protonation is hypothesized to regulate pH-dependent receptor recognition. Here, we systematically dissect its molecular origin by characterizing the consequences of His to Ala mutations on pH-dependent receptor-binding kinetics, site-specific histidine protonation, and high resolution structures of the intermolecular interface. Thermodynamic modeling of the pH dependence to receptor-binding affinity reveals large changes in site-specific protonation constants for a majority of interface histidines upon complexation. Removal of individual His imidazoles reduces these perturbations in protonation constants, which is most likely explained by the introduction of solvent-filled, buried cavities in the crystallographic structures without inducing significant conformational rearrangements.
-===A mutant human Prolactin receptor antagonist H180A in complex with the extracellular domain of the human prolactin receptor===
+Two independent histidines, one in human prolactin and one in its receptor, are critical for pH dependent receptor recognition and activation.,Kulkarni MV, Tettamanzi MC, Murphy JW, Keeler C, Myszka DG, Chayen NE, Lolis EJ, Hodsdon ME J Biol Chem. 2010 Sep 30. PMID:20889499<ref>PMID:20889499</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3ncb" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_20889499}}, adds the Publication Abstract to the page
+*[[Prolactin|Prolactin]]
-(as it appears on PubMed at http://www.pubmed.gov), where 20889499 is the PubMed ID number.
+*[[Prolactin receptor|Prolactin receptor]]
--->
+== References ==
-{{ABSTRACT_PUBMED_20889499}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-NCB is a 2 chains structure with 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=3NCB OCA].
-==Reference==
-<ref group="xtra">PMID:20889499</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Chayen, N E.]]
+[[Category: Large Structures]]
-[[Category: Hodsdon, M E.]]
+[[Category: Chayen NE]]
-[[Category: Keeler, C.]]
+[[Category: Hodsdon ME]]
-[[Category: Kulkarni, M V.]]
+[[Category: Keeler C]]
-[[Category: Lolis, E J.]]
+[[Category: Kulkarni MV]]
-[[Category: Murphy, J W.]]
+[[Category: Lolis EJ]]
-[[Category: Myszka, D G.]]
+[[Category: Murphy JW]]
-[[Category: Tettamanzi, M C.]]
+[[Category: Myszka DG]]
-[[Category: Hematopoietic cytokine]]
+[[Category: Tettamanzi MC]]
-[[Category: Hormone-hormone receptor complex]]
-[[Category: Ph dependence]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 20 06:13:12 2010''