4idl

Publication Abstract from PubMed

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 beta-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.

Structure of a low-melting-temperature anti-cholera toxin: llama V(H)H domain.,Legler PM, Zabetakis D, Anderson GP, Lam A, Hol WG, Goldman ER Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Feb 1;69(Pt 2):90-3. doi: , 10.1107/S1744309112050750. Epub 2013 Jan 26. PMID:23385744^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.