The nature of antibody heavy chain residue H6 strongly influences the stability of a VH domain lacking the disulfide bridge.

@article{Langedijk1998TheNO,
  title={The nature of antibody heavy chain residue H6 strongly influences the stability of a VH domain lacking the disulfide bridge.},
  author={A C Langedijk and Annemarie Honegger and Jan Maat and Roelf Johannes Planta and Robert van Schaik and Andreas Pl{\"u}ckthun},
  journal={Journal of molecular biology},
  year={1998},
  volume={283 1},
  pages={
          95-110
        }
}
Monoclonal antibody mAb 03/01/01, directed against the musk odorant traseolide, carries a serine residue instead of the conserved Cys H92 in the heavy chain variable domain, and is thus lacking the highly conserved disulfide bridge. We investigated the energetic consequence of restoring the disulfide bond and the nature of residue H6 (Glu or Gln), which is poised to interact with Ser H92 in the recombinant scFv fragment obtained from this antibody. In the scFv fragment derived from this… 
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An unusual cysteine VL87 affects the antibody fragment conformations without interfering with the disulfide bond formation.
The importance of framework residues H6, H7 and H10 in antibody heavy chains: experimental evidence for a new structural subclassification of antibody V(H) domains.
TLDR
The N-terminal segment of the heavy chain of antibodies of antibodies shows significant conformational variability correlating with the nature of the amino acids H6, H7 and H10 (Kabat H9), and the causal relationship between the local sequence and the structure of this framework region is established.
Removal of the conserved disulfide bridges from the scFv fragment of an antibody: effects on folding kinetics and aggregation.
TLDR
The results show that refolding of all four scFvs is ultimately limited by a slow proline isomerization in the VLdomain, since the native cis -conformation of proline L95 seems to be a prerequisite for formation of the native interface.
The influence of the buried glutamine or glutamate residue in position 6 on the structure of immunoglobulin variable domains.
TLDR
The marked structural variability of the V(H) framework 1 region is caused by three residues: the buried side-chain of H6, which can be either a glutamate or a glutamine residue, the residue in position H7, which may be proline only if H6 is glutamine, and by H9 (H10 according to a new consensus nomenclature), which has to be either glycine or proline if H 6 is a glutamate residue.
Role of native-state topology in the stabilization of intracellular antibodies.
Altering the fine specificity of an anti-Legionella single chain antibody by a single amino acid insertion.
Functional mapping of conserved, surface‐exposed charges of antibody variable domains
TLDR
The role of residues remote from the interaction site in the recognition function as well as the limited effect of surface charge modifications in antibody fragments on kinetic interaction parameters are demonstrated.
N‐terminal mutations in the anti‐estradiol Fab 57‐2 modify its hapten binding properties
TLDR
Analysis of a newly determined crystal structure of the authentic Fab 57‐2 in complex with estradiol suggests that mutations in the residue 2 in VH, and 2 and 4 in the VL domain were those responsible for the observed effects, which imply that similar effects can occur with other recombinant antibodies as well.
Generation and characterization of a scFv against recombinant coat protein of the geminivirus tomato leaf curl New Delhi virus
TLDR
A hybridoma cell line secreting the monoclonal antibody (mAb) HAV, which recognizes the coat (AV1) protein of tomato leaf curl New Delhi virus (ToLCNDV), a begomovirus, is established, showing the importance of restoring the 21 N-terminal amino acids.
Minimal structural elements of an inhibitory anti-ATF1/CREB single-chain antibody fragment (scFv41.4).
TLDR
The single-chain antibody fragment scFv41.4 represents a unique molecule with potential for use in the design of peptidomimetic derivatives having therapeutic application to human cancer, and was verified that deletion of the light chain did not result in reduced inhibitory activity.
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Surprisingly, it is observed that under some refolding conditions, the unpaired cysteine residue of functional scFv of ABPC48 is derivatized by glutathione, which implies a very unusual conformation of stand b containing the unaired Cys H22, which might be stabilized by interactions with the tyrosine residue in position H92.
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TLDR
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