2q76: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2q76.jpg|left|200px]] | [[Image:2q76.jpg|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_2q76", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_2q76| PDB=2q76 | SCENE= }} | |||
}} | |||
'''Mouse anti-hen egg white lysozyme antibody F10.6.6 Fab fragment''' | '''Mouse anti-hen egg white lysozyme antibody F10.6.6 Fab fragment''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q76 OCA]. | |||
==Reference== | ==Reference== | ||
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] | 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] | ||
[[Category: Acierno, J P.]] | [[Category: Acierno, J P.]] | ||
[[Category: Braden, B C.]] | [[Category: Braden, B C.]] | ||
| Line 30: | Line 25: | ||
[[Category: Goldbaum, F A.]] | [[Category: Goldbaum, F A.]] | ||
[[Category: Klinke, S.]] | [[Category: Klinke, S.]] | ||
[[Category: | [[Category: Affinity maturation]] | ||
[[Category: | [[Category: Antibody]] | ||
[[Category: | [[Category: Fab fragment]] | ||
[[Category: | [[Category: Immune system]] | ||
[[Category: | [[Category: Lysozyme]] | ||
[[Category: | [[Category: Vh-vl interface.]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:28:07 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 14:28, 4 May 2008
Mouse anti-hen egg white lysozyme antibody F10.6.6 Fab fragment
OverviewOverview
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.
About this StructureAbout this Structure
Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sun May 4 14:28:07 2008