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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 255 617-27 (1996)
Cited: 8 times
EuropePMC logo PMID: 8568901

Abstract

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.

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  2. A complete, multi-level conformational clustering of antibody complementarity-determining regions. Nikoloudis D, Pitts JE, Saldanha JW. PeerJ 2 e456 (2014)


Articles citing this publication (6)

  1. Analysis of the antigen combining site: correlations between length and sequence composition of the hypervariable loops and the nature of the antigen. Collis AV, Brouwer AP, Martin AC. J Mol Biol 325 337-354 (2003)
  2. Functional mimicry: elicitation of a monoclonal anti-idiotypic antibody hydrolizing beta-lactams. Avalle B, Thomas D, Friboulet A. FASEB J 12 1055-1060 (1998)
  3. Llama single domain antibodies as a tool for molecular mimicry. Zarebski LM, Urrutia M, Goldbaum FA. J Mol Biol 349 814-824 (2005)
  4. The promise of the anti-idiotype concept. Kieber-Emmons T, Monzavi-Karbassi B, Pashov A, Saha S, Murali R, Kohler H. Front Oncol 2 196 (2012)
  5. Molecular imprint of enzyme active site by camel nanobodies: rapid and efficient approach to produce abzymes with alliinase activity. Li JW, Xia L, Su Y, Liu H, Xia X, Lu Q, Yang C, Reheman K. J Biol Chem 287 13713-13721 (2012)
  6. The structure of an antitumor C(H)2-domain-deleted humanized antibody. Larson SB, Day JS, Glaser S, Braslawsky G, McPherson A. J Mol Biol 348 1177-1190 (2005)


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