1ol9: Difference between revisions

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 {{Theoretical_model}}
-{{Seed}}
-[[Image:1ol9.png|left|200px]]
-<!--
+==EPIBATIDINE BOUND ON A MODEL OF CHICK ALPHA7 NICOTINIC RECEPTORS==
-The line below this paragraph, containing "STRUCTURE_1ol9", creates the "Structure Box" on the page.
+<StructureSection load='1ol9' size='340' side='right'caption='[[1ol9]]' 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=1OL9 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=1ol9 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1ol9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ol9 ProSAT]</span></td></tr>
--->
+</table>
-{{STRUCTURE_1ol9|  PDB=1ol9  |  SCENE=  }}
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We constructed a three-dimensional model of the amino-terminal extracellular domain of three major types of nicotinic acetylcholine receptor, (alpha7)5, (alpha4)2(beta2)3, and (alpha1)2beta1gammadelta, on the basis of the recent x-ray structure determination of the molluscan acetylcholine-binding protein. Comparative analysis of the three models reveals that the agonist-binding pocket is much more conserved than the overall structure. Differences exist, however, in the side chains of several residues. In particular, a phenylalanine residue, present in beta2 but not in alpha7, is proposed to contribute to the high affinity for agonists in receptors containing the beta2 subunit. The semiautomatic docking of agonists in the ligand-binding pocket of (alpha7)5 led to positions consistent with labeling and mutagenesis experiments. Accordingly, the quaternary ammonium head group of nicotine makes a pi-cation interaction with W148 (alpha7 numbering), whereas the pyridine ring is close to both the cysteine pair 189-190 and the complementary component of the binding site. The intrinsic affinities inferred from docking give a rank order epibatidine &gt; nicotine &gt; acetylcholine, in agreement with experimental values. Finally, our models offer a structural basis for potentiation by external Ca2+.
-===EPIBATIDINE BOUND ON A MODEL OF CHICK ALPHA7 NICOTINIC RECEPTORS===
+Models of the extracellular domain of the nicotinic receptors and of agonist- and Ca2+-binding sites.,Le Novere N, Grutter T, Changeux JP Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):3210-5. Epub 2002 Feb 26. PMID:11867716<ref>PMID:11867716</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_11867716}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1ol9" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11867716 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11867716}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Theoretical Model]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OL9 OCA].
+[[Category: Large Structures]]
-==Reference==
-<ref group="xtra">PMID:11867716</ref><references group="xtra"/>
 [[Category: Le Novere, N]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 09:08:21 2010''