2ihl
From Proteopedia
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| - | [[Image:2ihl.gif|left|200px]]<br /><applet load="2ihl" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2ihl, resolution 1.4Å" /> | ||
| - | '''LYSOZYME (E.C.3.2.1.17) (JAPANESE QUAIL)'''<br /> | ||
| - | == | + | ==LYSOZYME (E.C.3.2.1.17) (JAPANESE QUAIL)== |
| + | <StructureSection load='2ihl' size='340' side='right'caption='[[2ihl]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2ihl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Coturnix_japonica Coturnix japonica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IHL 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]] 1.4Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=2ihl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ihl OCA], [https://pdbe.org/2ihl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ihl RCSB], [https://www.ebi.ac.uk/pdbsum/2ihl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ihl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LYSC_COTJA LYSC_COTJA] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. | ||
| + | == 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/ih/2ihl_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=2ihl ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Although antibodies are highly specific, cross-reactions are frequently observed. To understand the molecular basis of this phenomenon, we studied the anti-hen egg lysozyme (HEL) monoclonal antibody (mAb) D11.15, which cross-reacts with several avian lysozymes, in some cases with a higher affinity (heteroclitic binding) than for HEL. We have determined the crystal structure of the Fv fragment of D11.15 complexed with pheasant egg lysozyme (PHL). In addition, we have determined the structure of PHL, Guinea fowl egg lysozyme, and Japanese quail egg lysozyme. Differences in the affinity of D11.15 for the lysozymes appear to result from sequence substitutions in these antigens at the interface with the antibody. More generally, cross-reactivity is seen to require a stereochemically permissive environment for the variant antigen residues at the antibody-antigen interface. | Although antibodies are highly specific, cross-reactions are frequently observed. To understand the molecular basis of this phenomenon, we studied the anti-hen egg lysozyme (HEL) monoclonal antibody (mAb) D11.15, which cross-reacts with several avian lysozymes, in some cases with a higher affinity (heteroclitic binding) than for HEL. We have determined the crystal structure of the Fv fragment of D11.15 complexed with pheasant egg lysozyme (PHL). In addition, we have determined the structure of PHL, Guinea fowl egg lysozyme, and Japanese quail egg lysozyme. Differences in the affinity of D11.15 for the lysozymes appear to result from sequence substitutions in these antigens at the interface with the antibody. More generally, cross-reactivity is seen to require a stereochemically permissive environment for the variant antigen residues at the antibody-antigen interface. | ||
| - | + | Three-dimensional structure of a heteroclitic antigen-antibody cross-reaction complex.,Chitarra V, Alzari PM, Bentley GA, Bhat TN, Eisele JL, Houdusse A, Lescar J, Souchon H, Poljak RJ Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7711-5. PMID:8356074<ref>PMID:8356074</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2ihl" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Lysozyme 3D structures|Lysozyme 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Coturnix japonica]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bentley GA]] | ||
| + | [[Category: Houdusse A]] | ||
| + | [[Category: Poljak RJ]] | ||
| + | [[Category: Souchon H]] | ||
| + | [[Category: Zhang Z]] | ||
Current revision
LYSOZYME (E.C.3.2.1.17) (JAPANESE QUAIL)
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