2q76: Difference between revisions

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New page: left|200px {{Structure |PDB= 2q76 |SIZE=350|CAPTION= <scene name='initialview01'>2q76</scene>, resolution 2.00Å |SITE= |LIGAND= |ACTIVITY= |GENE= }} '''Mous...
 
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[[Image:2q76.jpg|left|200px]]


{{Structure
==Mouse anti-hen egg white lysozyme antibody F10.6.6 Fab fragment==
|PDB= 2q76 |SIZE=350|CAPTION= <scene name='initialview01'>2q76</scene>, resolution 2.00&Aring;
<StructureSection load='2q76' size='340' side='right'caption='[[2q76]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[2q76]] is a 4 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=2Q76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q76 FirstGlance]. <br>
|ACTIVITY=  
</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&#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=2q76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q76 OCA], [https://pdbe.org/2q76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q76 RCSB], [https://www.ebi.ac.uk/pdbsum/2q76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q76 ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/IGKC_MOUSE IGKC_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/q7/2q76_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=2q76 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The somatic mutations accumulated in variable and framework regions of antibodies produce structural changes that increase the affinity towards the antigen. This implies conformational and non covalent bonding changes at the paratope, as well as possible quaternary structure changes and rearrangements at the V(H)-V(L) interface. The consequences of the affinity maturation on the stability of the Fv domain were studied in a system composed of two closely related antibodies, F10.6.6 and D44.1, which recognize the same hen egg-white lysozyme (HEL) epitope. The mAb F10.6.6 has an affinity constant 700 times higher than D44.1, due to a higher surface complementarity to HEL. The structure of the free form of the Fab F10.6.6 presented here allows a comparative study of the conformational changes produced upon binding to antigen. By means of structural comparison, kinetics and thermodynamics of binding and stability studies on Fab and Fv fragments of both antibodies, we have determined that the affinity maturation process of anti-protein antibodies affects the shape of the combining site and the secondary structure content of the variable domain, stabilizes the V(H)-V(L) interaction, and consequently produces an increase of the Fv domain stability, improving the binding to antigen.


'''Mouse anti-hen egg white lysozyme antibody F10.6.6 Fab fragment'''
Affinity maturation increases the stability and plasticity of the Fv domain of anti-protein antibodies.,Acierno JP, Braden BC, Klinke S, Goldbaum FA, Cauerhff A J Mol Biol. 2007 Nov 16;374(1):130-46. Epub 2007 Sep 11. PMID:17916365<ref>PMID:17916365</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2q76" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The somatic mutations accumulated in variable and framework regions of antibodies produce structural changes that increase the affinity towards the antigen. This implies conformational and non covalent bonding changes at the paratope, as well as possible quaternary structure changes and rearrangements at the V(H)-V(L) interface. The consequences of the affinity maturation on the stability of the Fv domain were studied in a system composed of two closely related antibodies, F10.6.6 and D44.1, which recognize the same hen egg-white lysozyme (HEL) epitope. The mAb F10.6.6 has an affinity constant 700 times higher than D44.1, due to a higher surface complementarity to HEL. The structure of the free form of the Fab F10.6.6 presented here allows a comparative study of the conformational changes produced upon binding to antigen. By means of structural comparison, kinetics and thermodynamics of binding and stability studies on Fab and Fv fragments of both antibodies, we have determined that the affinity maturation process of anti-protein antibodies affects the shape of the combining site and the secondary structure content of the variable domain, stabilizes the V(H)-V(L) interaction, and consequently produces an increase of the Fv domain stability, improving the binding to antigen.
*[[Antibody 3D structures|Antibody 3D structures]]
 
*[[Sandbox 20009|Sandbox 20009]]
==About this Structure==
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
2Q76 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q76 OCA].
== References ==
 
<references/>
==Reference==
__TOC__
Affinity maturation increases the stability and plasticity of the Fv domain of anti-protein antibodies., Acierno JP, Braden BC, Klinke S, Goldbaum FA, Cauerhff A, J Mol Biol. 2007 Nov 16;374(1):130-46. Epub 2007 Sep 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17916365 17916365]
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Acierno JP]]
[[Category: Acierno, J P.]]
[[Category: Braden BC]]
[[Category: Braden, B C.]]
[[Category: Cauerhff A]]
[[Category: Cauerhff, A.]]
[[Category: Goldbaum FA]]
[[Category: Goldbaum, F A.]]
[[Category: Klinke S]]
[[Category: Klinke, S.]]
[[Category: affinity maturation]]
[[Category: antibody]]
[[Category: fab fragment]]
[[Category: immune system]]
[[Category: lysozyme]]
[[Category: vh-vl interface.]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:22:36 2008''

Latest revision as of 10:45, 9 October 2024

Mouse anti-hen egg white lysozyme antibody F10.6.6 Fab fragmentMouse anti-hen egg white lysozyme antibody F10.6.6 Fab fragment

Structural highlights

2q76 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IGKC_MOUSE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The somatic mutations accumulated in variable and framework regions of antibodies produce structural changes that increase the affinity towards the antigen. This implies conformational and non covalent bonding changes at the paratope, as well as possible quaternary structure changes and rearrangements at the V(H)-V(L) interface. The consequences of the affinity maturation on the stability of the Fv domain were studied in a system composed of two closely related antibodies, F10.6.6 and D44.1, which recognize the same hen egg-white lysozyme (HEL) epitope. The mAb F10.6.6 has an affinity constant 700 times higher than D44.1, due to a higher surface complementarity to HEL. The structure of the free form of the Fab F10.6.6 presented here allows a comparative study of the conformational changes produced upon binding to antigen. By means of structural comparison, kinetics and thermodynamics of binding and stability studies on Fab and Fv fragments of both antibodies, we have determined that the affinity maturation process of anti-protein antibodies affects the shape of the combining site and the secondary structure content of the variable domain, stabilizes the V(H)-V(L) interaction, and consequently produces an increase of the Fv domain stability, improving the binding to antigen.

Affinity maturation increases the stability and plasticity of the Fv domain of anti-protein antibodies.,Acierno JP, Braden BC, Klinke S, Goldbaum FA, Cauerhff A J Mol Biol. 2007 Nov 16;374(1):130-46. Epub 2007 Sep 11. PMID:17916365[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Acierno JP, Braden BC, Klinke S, Goldbaum FA, Cauerhff A. Affinity maturation increases the stability and plasticity of the Fv domain of anti-protein antibodies. J Mol Biol. 2007 Nov 16;374(1):130-46. Epub 2007 Sep 11. PMID:17916365 doi:10.1016/j.jmb.2007.09.005

2q76, resolution 2.00Å

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