2q76

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{{STRUCTURE_2q76| PDB=2q76 | SCENE= }}
{{STRUCTURE_2q76| PDB=2q76 | SCENE= }}
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'''Mouse anti-hen egg white lysozyme antibody F10.6.6 Fab fragment'''
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===Mouse anti-hen egg white lysozyme antibody F10.6.6 Fab fragment===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17916365 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17916365}}
==About this Structure==
==About this Structure==
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==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]
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Structural mechanism for affinity maturation of an anti-lysozyme antibody., Cauerhff A, Goldbaum FA, Braden BC, Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3539-44. Epub 2004 Feb 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14988501 14988501]
[[Category: Acierno, J P.]]
[[Category: Acierno, J P.]]
[[Category: Braden, B C.]]
[[Category: Braden, B C.]]
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[[Category: Lysozyme]]
[[Category: Lysozyme]]
[[Category: Vh-vl interface.]]
[[Category: Vh-vl interface.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:28:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:18:48 2008''

Revision as of 13:18, 29 July 2008

Image:2q76.png

Template:STRUCTURE 2q76

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

Template:ABSTRACT PUBMED 17916365

About this Structure

Full crystallographic information is available from OCA.

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:17916365

Structural mechanism for affinity maturation of an anti-lysozyme antibody., Cauerhff A, Goldbaum FA, Braden BC, Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3539-44. Epub 2004 Feb 26. PMID:14988501

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