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1em4

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1em4.png|left|200px]]
 
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==COMPUTATIONAL MODEL OF ANTIBODY 4D5 BOUND TO BENZO[A]PYRENE==
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The line below this paragraph, containing "STRUCTURE_1em4", creates the "Structure Box" on the page.
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<StructureSection load='1em4' size='340' side='right'caption='[[1em4]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EM4 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=1em4 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1em4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1em4 ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1em4| PDB=1em4 | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Proteins can use aromatic side-chains to stabilize bound cationic ligands through cation-pi interactions. Here, we report the first example of the reciprocal process, termed pi-cation, in which a cationic protein side-chain stabilizes a neutral aromatic ligand. Site-directed mutagenesis revealed that an arginine side-chain located in the deep binding pocket of a monoclonal antibody (4D5) is essential for binding the neutral polynuclear aromatic hydrocarbon benzo[a]pyrene. This Arg was very likely selected for in the primary response, further underscoring the importance of the pi-cation interaction for ligand binding, which should be considered in protein analysis and design when ligands include aromatic groups.
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===COMPUTATIONAL MODEL OF ANTIBODY 4D5 BOUND TO BENZO[A]PYRENE===
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Stabilization of bound polycyclic aromatic hydrocarbons by a pi-cation interaction.,Pellequer JL, Zhao B, Kao HI, Bell CW, Li K, Li QX, Karu AE, Roberts VA J Mol Biol. 2000 Sep 22;302(3):691-9. PMID:10986127<ref>PMID:10986127</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_10986127}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1em4" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10986127 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10986127}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EM4 OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:10986127</ref><references group="xtra"/>
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[[Category: Pellequer, J.-L]]
[[Category: Pellequer, J.-L]]
[[Category: Roberts, V A]]
[[Category: Roberts, V A]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 06:36:37 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

COMPUTATIONAL MODEL OF ANTIBODY 4D5 BOUND TO BENZO[A]PYRENE

PDB ID 1em4

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