1i3v: Difference between revisions

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[[Image:1i3v.gif|left|200px]]
{{Seed}}
[[Image:1i3v.png|left|200px]]


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{{STRUCTURE_1i3v|  PDB=1i3v  |  SCENE=  }}  
{{STRUCTURE_1i3v|  PDB=1i3v  |  SCENE=  }}  


'''THREE-DIMENSIONAL STRUCTURE OF A LAMA VHH DOMAIN UNLIGANDED'''
===THREE-DIMENSIONAL STRUCTURE OF A LAMA VHH DOMAIN UNLIGANDED===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11469862}}


==About this Structure==
==About this Structure==
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[[Category: Domain vhh]]
[[Category: Domain vhh]]
[[Category: Lama]]
[[Category: Lama]]
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Revision as of 07:22, 1 July 2008

File:1i3v.png

Template:STRUCTURE 1i3v

THREE-DIMENSIONAL STRUCTURE OF A LAMA VHH DOMAIN UNLIGANDED

Template:ABSTRACT PUBMED 11469862

About this Structure

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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