2eh7
From Proteopedia
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| - | [[Image:2eh7.jpg|left|200px]]<br /><applet load="2eh7" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2eh7, resolution 2.50Å" /> | ||
| - | '''Crystal structure of humanized KR127 FAB'''<br /> | ||
| - | == | + | ==Crystal structure of humanized KR127 FAB== |
| + | <StructureSection load='2eh7' size='340' side='right'caption='[[2eh7]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2eh7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EH7 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=2eh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eh7 OCA], [https://pdbe.org/2eh7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eh7 RCSB], [https://www.ebi.ac.uk/pdbsum/2eh7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eh7 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/eh/2eh7_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=2eh7 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The humanized monoclonal antibody HzKR127 recognizes the preS1 domain of the human hepatitis B virus surface proteins with a broadly neutralizing activity in vivo. We present the crystal structures of HzKR127 Fab and its complex with a major epitope peptide. In the complex structure, the bound peptide forms a type IV beta-turn followed by 3(10) helical turn, the looped-out conformation of which provides a structural basis for broad neutralization. Upon peptide binding, the antibody undergoes a dramatic complementarity determining region H3 lid opening. To understand the structural implication of the virus neutralization, we carried out comprehensive alanine-scanning mutagenesis of all complementarity determining region residues in HzKR127 Fab. The functional mapping of the antigen-combining site demonstrates the specific roles of major binding determinants in antigen binding, contributing to the rational design for maximal humanization and affinity maturation of the antibody. | The humanized monoclonal antibody HzKR127 recognizes the preS1 domain of the human hepatitis B virus surface proteins with a broadly neutralizing activity in vivo. We present the crystal structures of HzKR127 Fab and its complex with a major epitope peptide. In the complex structure, the bound peptide forms a type IV beta-turn followed by 3(10) helical turn, the looped-out conformation of which provides a structural basis for broad neutralization. Upon peptide binding, the antibody undergoes a dramatic complementarity determining region H3 lid opening. To understand the structural implication of the virus neutralization, we carried out comprehensive alanine-scanning mutagenesis of all complementarity determining region residues in HzKR127 Fab. The functional mapping of the antigen-combining site demonstrates the specific roles of major binding determinants in antigen binding, contributing to the rational design for maximal humanization and affinity maturation of the antibody. | ||
| - | + | Broadly neutralizing anti-hepatitis B virus antibody reveals a complementarity determining region H3 lid-opening mechanism.,Chi SW, Maeng CY, Kim SJ, Oh MS, Ryu CJ, Kim SJ, Han KH, Hong HJ, Ryu SE Proc Natl Acad Sci U S A. 2007 May 29;104(22):9230-5. Epub 2007 May 17. PMID:17517649<ref>PMID:17517649</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2eh7" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Antibody 3D structures|Antibody 3D structures]] | ||
| + | *[[Sandbox 20009|Sandbox 20009]] | ||
| + | *[[3D structures of non-human antibody|3D structures of non-human antibody]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Chi S-W]] | ||
| + | [[Category: Hong HJ]] | ||
| + | [[Category: Kim S-J]] | ||
| + | [[Category: Maeng C-Y]] | ||
| + | [[Category: Ryu S-E]] | ||
Current revision
Crystal structure of humanized KR127 FAB
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Categories: Large Structures | Mus musculus | Chi S-W | Hong HJ | Kim S-J | Maeng C-Y | Ryu S-E
