1GHF

ANTI-ANTI-IDIOTYPE GH1002 FAB FRAGMENT

Summary for 1GHF

• Entry DOI: 10.2210/pdb1ghf/pdb
• Descriptor: ANTI-ANTI-IDIOTYPE GH1002 FAB FRAGMENT (2 entities in total)
• Functional Keywords: antibody fab fragment
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 46538.76

Authors

Ban, N.,Day, J.,Wang, X.,Ferrone, S.,McPherson, A. (deposition date: 1995-11-30, release date: 1996-12-23, Last modification date: 2024-11-13)

Primary citation

Ban, N.,Day, J.,Wang, X.,Ferrone, S.,McPherson, A.
Crystal structure of an anti-anti-idiotype shows it to be self-complementary.
J.Mol.Biol., 255:617-627, 1996

PubMed 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.

PubMed: 8568901
DOI: 10.1006/jmbi.1996.0051

Experimental method

X-RAY DIFFRACTION (2.7 Å)