1dvf
From Proteopedia
(New page: 200px<br /> <applet load="1dvf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dvf, resolution 1.9Å" /> '''IDIOTOPIC ANTIBODY D...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1dvf.gif|left|200px]]<br /> | + | [[Image:1dvf.gif|left|200px]]<br /><applet load="1dvf" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1dvf" size=" | + | |
caption="1dvf, resolution 1.9Å" /> | caption="1dvf, resolution 1.9Å" /> | ||
'''IDIOTOPIC ANTIBODY D1.3 FV FRAGMENT-ANTIIDIOTOPIC ANTIBODY E5.2 FV FRAGMENT COMPLEX'''<br /> | '''IDIOTOPIC ANTIBODY D1.3 FV FRAGMENT-ANTIIDIOTOPIC ANTIBODY E5.2 FV FRAGMENT COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Anti-idiotopic antibodies react with unique antigenic features, usually | + | Anti-idiotopic antibodies react with unique antigenic features, usually associated with the combining sites, of other antibodies. They may thus mimic specific antigens that react with the same antibodies. The structural basis of this mimicry is analyzed here in detail for an anti-idiotopic antibody that mimics the antigen, hen egg-white lysozyme. The crystal structure of an anti-hen-egg-white lysozyme antibody (D1.3) complexed with an anti-idiotopic antibody (E5.2) has been determined at a nominal resolution of 1.9 A. E5.2 contacts substantially the same residues of D1.3 as lysozyme, thus mimicking its binding to D1.3. The mimicry embodies conservation of hydrogen bonding: six of the 14 protein-protein hydrogen bonds bridging D1.3-E5.2 are structurally equivalent to hydrogen bonds bridging D1.3-lysozyme. The mimicry includes a similar number of van der Waals interactions. The mimicry of E5.2 for lysozyme, however, does not extend to the topology of the non-polar surfaces of E5.2 and lysozyme, which are in contact with D1.3 as revealed by a quantitative analysis of the contacting surface similarities between E5.2 and lysozyme. The structure discussed herein shows that an anti-idiotopic antibody can provide an approximate topological and binding-group mimicry of an external antigen, especially in the case of the hydrophilic surfaces, even though there is no sequence homology between the anti-idiotope and the antigen. |
==About this Structure== | ==About this Structure== | ||
| - | 1DVF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1DVF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DVF OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 13: | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Acqua, W | + | [[Category: Acqua, W Dall.]] |
| - | [[Category: Braden, B | + | [[Category: Braden, B C.]] |
| - | [[Category: Fields, B | + | [[Category: Fields, B A.]] |
| - | [[Category: Goldbaum, F | + | [[Category: Goldbaum, F A.]] |
| - | [[Category: Mariuzza, R | + | [[Category: Mariuzza, R A.]] |
| - | [[Category: Poljak, R | + | [[Category: Poljak, R J.]] |
[[Category: Ysern, X.]] | [[Category: Ysern, X.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
| Line 25: | Line 24: | ||
[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:53 2008'' |
Revision as of 10:20, 21 February 2008
|
IDIOTOPIC ANTIBODY D1.3 FV FRAGMENT-ANTIIDIOTOPIC ANTIBODY E5.2 FV FRAGMENT COMPLEX
Overview
Anti-idiotopic antibodies react with unique antigenic features, usually associated with the combining sites, of other antibodies. They may thus mimic specific antigens that react with the same antibodies. The structural basis of this mimicry is analyzed here in detail for an anti-idiotopic antibody that mimics the antigen, hen egg-white lysozyme. The crystal structure of an anti-hen-egg-white lysozyme antibody (D1.3) complexed with an anti-idiotopic antibody (E5.2) has been determined at a nominal resolution of 1.9 A. E5.2 contacts substantially the same residues of D1.3 as lysozyme, thus mimicking its binding to D1.3. The mimicry embodies conservation of hydrogen bonding: six of the 14 protein-protein hydrogen bonds bridging D1.3-E5.2 are structurally equivalent to hydrogen bonds bridging D1.3-lysozyme. The mimicry includes a similar number of van der Waals interactions. The mimicry of E5.2 for lysozyme, however, does not extend to the topology of the non-polar surfaces of E5.2 and lysozyme, which are in contact with D1.3 as revealed by a quantitative analysis of the contacting surface similarities between E5.2 and lysozyme. The structure discussed herein shows that an anti-idiotopic antibody can provide an approximate topological and binding-group mimicry of an external antigen, especially in the case of the hydrophilic surfaces, even though there is no sequence homology between the anti-idiotope and the antigen.
About this Structure
1DVF is a Protein complex structure of sequences from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of an Fv-Fv idiotope-anti-idiotope complex at 1.9 A resolution., Braden BC, Fields BA, Ysern X, Dall'Acqua W, Goldbaum FA, Poljak RJ, Mariuzza RA, J Mol Biol. 1996 Nov 22;264(1):137-51. PMID:8950273
Page seeded by OCA on Thu Feb 21 12:20:53 2008
