Journal article

Single-chain Fv multimers of the anti-neuraminidase antibody NC10: the residue at position 15 in the V-L domain of the scFv-0 (V-L-V-H) molecule is primarily responsible for formation of a tetramer-trimer equilibrium

O Dolezal, R De Gori, M Walter, L Doughty, M Hattarki, PJ Hudson, AA Kortt

Protein Engineering Design and Selection | OXFORD UNIV PRESS | Published : 2003

Abstract

Single-chain variable fragment of the murine monoclonal antibody NC10 specific to influenza virus N9 neuraminidase, joined directly in the V(L) to V(H) orientation (scFv-0), forms an equilibrium mixture of tetramer and trimer with the tetramer as the preferred multimeric species. In contrast, the V(H)-V(L) isomer was previously shown to exist exclusively as a trimer. Computer-generated trimeric and tetrameric scFv models, based on the refined crystal structure for NC10 Fv domain, were constructed and used to evaluate factors influencing the transition between V(L)-V(H) trimer and tetramer. These model structures indicated that steric restrictions between loops spanning amino acid residues L5..

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