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Updated: May 14, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
Published on: September 15, 2010
Structure of a low-melting-temperature anti-cholera toxin: llama V(H)H domain
Patricia M Legler1, Dan Zabetakis, George P Anderson
1Center 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.
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