1ghf
From Proteopedia
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+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ghf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ghf OCA], [http://www.ebi.ac.uk/pdbsum/1ghf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ghf RCSB]</span> | ||
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[[Category: antibody fab fragment]] | [[Category: antibody fab fragment]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:44:02 2008'' |
Revision as of 17:44, 30 March 2008
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, resolution 2.7Å | |||||||
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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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