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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Feb 1;69(Pt 2):90-3. doi: 10.1107/S1744309112050750. Epub 2013 Jan 26.

Structure of a low-melting-temperature anti-cholera toxin: llama V(H)H domain.

Author information

1
Center for Bio/Molecular Science and Engineering, Naval Research Laboratory, Washington, DC 20375, USA. patricia.legler@nrl.navy.mil

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.

KEYWORDS:

cholera toxin; single-domain antibodies; thermal stability

PMID:
23385744
PMCID:
PMC3564605
DOI:
10.1107/S1744309112050750
[Indexed for MEDLINE]
Free PMC Article
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