1lmk
From Proteopedia
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THE STRUCTURE OF A BIVALENT DIABODY
Overview
BACKGROUND: 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. RESULTS: The 2.6 A resolution structure has been determined for a, bivalent diabody with a flexible five-residue polypeptide linker between, the (amino-terminal) VH and (carboxy-terminal) VL domains. The asymmetric, unit of the crystal consists of four polypeptides comprising two, diabodies; for one of these polypeptides the linker can be traced between, the VH and VL domains. Within each diabody the two associated VH and VL, domains make back-to-back interactions through the VH domains, and there, is an extensive VL-VL interface between the two diabodies in the, asymmetric unit. CONCLUSIONS: The structure of the diabody is very similar, to that which had been predicted by molecular modelling. Diabodies, directed against cell-surface antigens should be capable of bringing, together two cells, such as in cell-targeted therapy, because the two, antigen-binding sites of the diabody are at opposite ends of the molecule, and separated by approximately 65 A.
About this Structure
1LMK is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a diabody, a bivalent antibody fragment., Perisic O, Webb PA, Holliger P, Winter G, Williams RL, Structure. 1994 Dec 15;2(12):1217-26. PMID:7704531
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