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1LMK

THE STRUCTURE OF A BIVALENT DIABODY

Summary for 1LMK
Entry DOI10.2210/pdb1lmk/pdb
DescriptorANTI-PHOSPHATIDYLINOSITOL SPECIFIC PHOSPHOLIPASE C DIABODY (2 entities in total)
Functional Keywordsimmunoglobulin, diabody, single-chain fv, scfv
Biological sourceMus musculus (house mouse)
Total number of polymer chains4
Total formula weight104312.48
Authors
Williams, R.L. (deposition date: 1994-08-29, release date: 1995-03-31, Last modification date: 2024-10-30)
Primary citationPerisic, 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: 7704531
DOI: 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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