ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Structure of a low-melting-temperature anti-cholera toxin: llama V(H)H domain.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed.
- Attenuating ETEC virulence using a heat-labile enterotoxin-blocking binding protein.Gut microbes · 2026Article
- Orally delivered toxin-binding protein protects against diarrhoea in a murine cholera model.Nature communications · 2025Article
- TEMPRO: nanobody melting temperature estimation model using protein embeddings.Scientific reports · 2024Article
- Enhanced Conformational Sampling of Nanobody CDR H3 Loop by Generalized Replica-Exchange with Solute Tempering.Life (Basel, Switzerland) · 2021Article
- Experimental evaluation of single-domain antibodies predicted by molecular dynamics simulations to have elevated thermal stability.Protein science : a publication of the Protein Society · 2019Article
- Thermal stability of single-domain antibodies estimated by molecular dynamics simulations.Protein science : a publication of the Protein Society · 2019Article
- Chromatibody, a novel non-invasive molecular tool to explore and manipulate chromatin in living cells.Journal of cell science · 2016Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Variable heavy domains derived from the heavy-chain-only antibodies found in camelids (V(H)H domains) are known for their thermal stability. Here, the structure of A9, an anti-cholera toxin V(H)H domain (K(d) = 77 ± 5 nM) that has an unusually low melting temperature of 319.9 ± 1.6 K, is reported. The CDR3 residues of A9 form a β-hairpin that is directed away from the former V(H)-V(L) interfacial surface, exposing hydrophobic residues to the solvent. A DALI structural similarity search showed that this CDR3 conformation is uncommon.
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