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1ghf
From Proteopedia
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[[Image:1ghf.gif|left|200px]] | [[Image:1ghf.gif|left|200px]] | ||
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'''ANTI-ANTI-IDIOTYPE GH1002 FAB FRAGMENT''' | '''ANTI-ANTI-IDIOTYPE GH1002 FAB FRAGMENT''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHF OCA]. | |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/8568901 8568901] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8568901 8568901] | ||
| - | [[Category: Mus musculus]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Ban, N.]] | [[Category: Ban, N.]] | ||
[[Category: Day, J.]] | [[Category: Day, J.]] | ||
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[[Category: McPherson, A.]] | [[Category: McPherson, A.]] | ||
[[Category: Wang, X.]] | [[Category: Wang, X.]] | ||
| - | [[Category: | + | [[Category: Antibody fab fragment]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:33:51 2008'' | |
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Revision as of 14:33, 2 May 2008
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
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 Page seeded by OCA on Fri May 2 17:33:51 2008
