1i3v

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spinqualitylabelsall models 1i3v, resolution 2.03Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THREE-DIMENSIONAL STRUCTURE OF A LAMA VHH DOMAIN UNLIGANDED

Overview

Camelids, camels and llamas, have a unique immune system able to produce, heavy-chain only antibodies. Their VH domains (VHHs) are the smallest, binding units produced by immune systems, and therefore suitable for, biotechnological applications through heterologous expression. The, recognition of protein antigens by these VHHs is rather well documented, while less is known about the VHH/hapten interactions. The recently, reported X-ray structure of a VHH in complex with a copper-containing, azo-dye settled the ability of VHH to recognize haptens by forming a, cavity between the three complementarity-determining regions (CDR). Here, we report the structures of a VHH (VHH A52) free or complexed with an, azo-dye, RR1, without metal ion. The structure of the complex illustrates, the involvement of CDR2, CDR3 and a framework residue in a lateral, interaction with the hapten. Such a lateral combining site is comparable, to that found in classical antibodies, although in the absence of the VL.

About this Structure

1I3V is a Protein complex structure of sequences from Lama glama. Full crystallographic information is available from OCA.

Reference

Lateral recognition of a dye hapten by a llama VHH domain., Spinelli S, Tegoni M, Frenken L, van Vliet C, Cambillau C, J Mol Biol. 2001 Aug 3;311(1):123-9. PMID:11469862

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