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[[Image:1jhl.jpg|left|200px]]
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{{STRUCTURE_1jhl|  PDB=1jhl  |  SCENE=  }}
'''THREE-DIMENSIONAL STRUCTURE OF A HETEROCLITIC ANTIGEN-ANTIBODY CROSS-REACTION COMPLEX'''


==THREE-DIMENSIONAL STRUCTURE OF A HETEROCLITIC ANTIGEN-ANTIBODY CROSS-REACTION COMPLEX==
<StructureSection load='1jhl' size='340' side='right'caption='[[1jhl]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jhl]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Phasianus_colchicus Phasianus colchicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JHL 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]] 2.4&#8491;</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=1jhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jhl OCA], [https://pdbe.org/1jhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jhl RCSB], [https://www.ebi.ac.uk/pdbsum/1jhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jhl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LYSC_PHACO LYSC_PHACO] 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/jh/1jhl_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=1jhl 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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1JHL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Phasianus_colchicus Phasianus colchicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHL OCA].
</div>
<div class="pdbe-citations 1jhl" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/8356074 8356074]
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Phasianus colchicus]]
[[Category: Phasianus colchicus]]
[[Category: Protein complex]]
[[Category: Alzari PM]]
[[Category: Alzari, P M.]]
[[Category: Bentley GA]]
[[Category: Bentley, G A.]]
[[Category: Bhat TN]]
[[Category: Bhat, T N.]]
[[Category: Chitarra V]]
[[Category: Chitarra, V.]]
[[Category: Eisele J-L]]
[[Category: Eisele, J L.]]
[[Category: Poljak RJ]]
[[Category: Poljak, R J.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:13:57 2008''