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2q76

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Revision as of 07:48, 9 March 2022

Mouse 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.
Related:	1p2c, 1mlb, 1mlc
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

References

↑ 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

1 Structural highlights
2 Evolutionary Conservation
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2q76"

@@ Line 3: / Line 3: @@
 <StructureSection load='2q76' size='340' side='right'caption='[[2q76]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2q76]] is a 4 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2Q76 FirstGlance]. <br>
+<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>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p2c|1p2c]], [[1mlb|1mlb]], [[1mlc|1mlc]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1p2c|1p2c]], [[1mlb|1mlb]], [[1mlc|1mlc]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2q76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q76 OCA], [http://pdbe.org/2q76 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q76 RCSB], [http://www.ebi.ac.uk/pdbsum/2q76 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q76 ProSAT]</span></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=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>
 == Evolutionary Conservation ==
@@ Line 29: / Line 29: @@
 ==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/>

2q76

From Proteopedia

Revision as of 07:48, 9 March 2022

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

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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