1ghf
From Proteopedia
(New page: 200px<br /> <applet load="1ghf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ghf, resolution 2.7Å" /> '''ANTI-ANTI-IDIOTYPE G...) |
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| - | [[Image:1ghf.gif|left|200px]]<br /> | + | [[Image:1ghf.gif|left|200px]]<br /><applet load="1ghf" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ghf" size=" | + | |
caption="1ghf, resolution 2.7Å" /> | caption="1ghf, resolution 2.7Å" /> | ||
'''ANTI-ANTI-IDIOTYPE GH1002 FAB FRAGMENT'''<br /> | '''ANTI-ANTI-IDIOTYPE GH1002 FAB FRAGMENT'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of the Fab fragment of the mouse anti-anti-idiotypic | + | The structure of the Fab fragment of the mouse anti-anti-idiotypic monoclonal antibody (mAb) GH1002 was solved by X-ray crystallography. mAb GH1002 was elicited with the syngeneic anti-idiotype mAb MK2-23 which mimics the determinant defined by anti-human high molecular weight-melanoma associated antigen (HMW-MAA) mAb 763.74. The Fab fragments of mAb GH1002 exist in the crystal as dimers related by crystallographic 2-fold axes. The interface between dyad-related Fab fragments is formed primarily by interaction of the hypervariable loops of one with the other. The self-interaction of Fab fragments of anti-anti-idiotypic mAb GH1002 through their combining sites is extremely tight and intricate, closely resembling that observed in structures of id-anti-id complexes, and comparable in terms of total contact area, charge complementarity, and number of hydrogen bonds. The self-complementarity of the antibody observed here could be coincidental and thus reflect some non-specific binding capability. It might, on the other hand, be immunologically relevant and exemplify a certain degree of evolved self complementarity characteristic of antibodies participating in idiotypic cascades. |
==About this Structure== | ==About this Structure== | ||
| - | 1GHF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | + | 1GHF is a [http://en.wikipedia.org/wiki/Protein_complex 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=1GHF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: antibody fab fragment]] | [[Category: antibody fab fragment]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:04 2008'' |
Revision as of 10:50, 21 February 2008
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ANTI-ANTI-IDIOTYPE GH1002 FAB FRAGMENT
Overview
The structure of the Fab fragment of the mouse anti-anti-idiotypic monoclonal antibody (mAb) GH1002 was solved by X-ray crystallography. mAb GH1002 was elicited with the syngeneic anti-idiotype mAb MK2-23 which mimics the determinant defined by anti-human high molecular weight-melanoma associated antigen (HMW-MAA) mAb 763.74. The Fab fragments of mAb GH1002 exist in the crystal as dimers related by crystallographic 2-fold axes. The interface between dyad-related Fab fragments is formed primarily by interaction of the hypervariable loops of one with the other. The self-interaction of Fab fragments of anti-anti-idiotypic mAb GH1002 through their combining sites is extremely tight and intricate, closely resembling that observed in structures of id-anti-id complexes, and comparable in terms of total contact area, charge complementarity, and number of hydrogen bonds. The self-complementarity of the antibody observed here could be coincidental and thus reflect some non-specific binding capability. It might, on the other hand, be immunologically relevant and exemplify a certain degree of evolved self complementarity characteristic of antibodies participating in idiotypic cascades.
About this Structure
1GHF is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of an anti-anti-idiotype shows it to be self-complementary., Ban N, Day J, Wang X, Ferrone S, McPherson A, J Mol Biol. 1996 Feb 2;255(4):617-27. PMID:8568901
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