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[[Image:1j1o.gif|left|200px]]


{{Structure
==Crystal Structure of HyHEL-10 Fv mutant LY50F complexed with hen egg white lysozyme==
|PDB= 1j1o |SIZE=350|CAPTION= <scene name='initialview01'>1j1o</scene>, resolution 1.8&Aring;
<StructureSection load='1j1o' size='340' side='right'caption='[[1j1o]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1j1o]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J1O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J1O FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1j1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j1o OCA], [https://pdbe.org/1j1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j1o RCSB], [https://www.ebi.ac.uk/pdbsum/1j1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j1o ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/KV5A9_MOUSE KV5A9_MOUSE]
== 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/j1/1j1o_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=1j1o ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
To study the role of hydrogen bonding via interfacial water molecules in protein-protein interactions, we examined the interaction between hen egg white lysozyme (HEL) and its HyHEL-10 variable domain fragment (Fv) antibody. We constructed three antibody mutants (l-Y50F, l-S91A, and l-S93A) and investigated the interactions between the mutant Fvs and HEL. Isothermal titration calorimetry indicated that the mutations significantly decreased the negative enthalpy change (8-25 kJ mol(-1)), despite some offset by a favorable entropy change. X-ray crystallography demonstrated that the complexes had nearly identical structures, including the positions of the interfacial water molecules. Taken together, the isothermal titration calorimetric and x-ray crystallographic results indicate that hydrogen bonding via interfacial water enthalpically contributes to the Fv-HEL interaction despite the partial offset because of entropy loss, suggesting that hydrogen bonding stiffens the antigen-antibody complex.


'''Crystal Structure of HyHEL-10 Fv mutant LY50F complexed with hen egg white lysozyme'''
The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. The HyHEL-10-HEL interaction.,Yokota A, Tsumoto K, Shiroishi M, Kondo H, Kumagai I J Biol Chem. 2003 Feb 14;278(7):5410-8. Epub 2002 Nov 19. PMID:12444085<ref>PMID:12444085</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1j1o" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
To study the role of hydrogen bonding via interfacial water molecules in protein-protein interactions, we examined the interaction between hen egg white lysozyme (HEL) and its HyHEL-10 variable domain fragment (Fv) antibody. We constructed three antibody mutants (l-Y50F, l-S91A, and l-S93A) and investigated the interactions between the mutant Fvs and HEL. Isothermal titration calorimetry indicated that the mutations significantly decreased the negative enthalpy change (8-25 kJ mol(-1)), despite some offset by a favorable entropy change. X-ray crystallography demonstrated that the complexes had nearly identical structures, including the positions of the interfacial water molecules. Taken together, the isothermal titration calorimetric and x-ray crystallographic results indicate that hydrogen bonding via interfacial water enthalpically contributes to the Fv-HEL interaction despite the partial offset because of entropy loss, suggesting that hydrogen bonding stiffens the antigen-antibody complex.
*[[Lysozyme 3D structures|Lysozyme 3D structures]]
 
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
==About this Structure==
== References ==
1J1O is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J1O OCA].
<references/>
 
__TOC__
==Reference==
</StructureSection>
The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. The HyHEL-10-HEL interaction., Yokota A, Tsumoto K, Shiroishi M, Kondo H, Kumagai I, J Biol Chem. 2003 Feb 14;278(7):5410-8. Epub 2002 Nov 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12444085 12444085]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Lysozyme]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Kondo H]]
[[Category: Kondo, H.]]
[[Category: Kumagai I]]
[[Category: Kumagai, I.]]
[[Category: Shiroishi M]]
[[Category: Shiroishi, M.]]
[[Category: Tsumoto K]]
[[Category: Tsumoto, K.]]
[[Category: Yokota A]]
[[Category: Yokota, A.]]
[[Category: antigen-antibody complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:57:48 2008''

Latest revision as of 08:32, 6 November 2024

Crystal Structure of HyHEL-10 Fv mutant LY50F complexed with hen egg white lysozyme

1j1o, resolution 1.80Å

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