Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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