1LMK
THE STRUCTURE OF A BIVALENT DIABODY
Summary for 1LMK
| Entry DOI | 10.2210/pdb1lmk/pdb |
| Descriptor | ANTI-PHOSPHATIDYLINOSITOL SPECIFIC PHOSPHOLIPASE C DIABODY (2 entities in total) |
| Functional Keywords | immunoglobulin, diabody, single-chain fv, scfv |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 4 |
| Total formula weight | 104312.48 |
| Authors | Williams, R.L. (deposition date: 1994-08-29, release date: 1995-03-31, Last modification date: 2024-10-30) |
| Primary citation | Perisic, O.,Webb, P.A.,Holliger, P.,Winter, G.,Williams, R.L. Crystal structure of a diabody, a bivalent antibody fragment. Structure, 2:1217-1226, 1994 Cited by PubMed Abstract: Diabodies are dimeric antibody fragments. In each polypeptide, a heavy-chain variable domain (VH) is linked to a light-chain variable domain (VL) but unlike single-chain Fv fragments, each antigen-binding site is formed by pairing of one VH and one VL domain from the two different polypeptides. Diabodies thus have two antigen-binding sites, and can be bispecific. Direct structural evidence is lacking for the connections and dimeric interactions between the two polypeptides of the diabody. PubMed: 7704531DOI: 10.1016/S0969-2126(94)00123-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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