1qd0
From Proteopedia
(New page: 200px<br /> <applet load="1qd0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qd0, resolution 2.50Å" /> '''CAMELID HEAVY CHAIN...) |
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| - | [[Image:1qd0.gif|left|200px]]<br /> | + | [[Image:1qd0.gif|left|200px]]<br /><applet load="1qd0" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1qd0" size=" | + | |
caption="1qd0, resolution 2.50Å" /> | caption="1qd0, resolution 2.50Å" /> | ||
'''CAMELID HEAVY CHAIN VARIABLE DOMAINS PROVIDE EFFICIENT COMBINING SITES TO HAPTENS'''<br /> | '''CAMELID HEAVY CHAIN VARIABLE DOMAINS PROVIDE EFFICIENT COMBINING SITES TO HAPTENS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Camelids can produce antibodies devoid of light chains and CH1 domains | + | Camelids can produce antibodies devoid of light chains and CH1 domains (Hamers-Casterman, C. et al. (1993) Nature 363, 446-448). Camelid heavy-chain variable domains (VHH) have high affinities for protein antigens and the structures of two of these complexes have been determined (Desmyter, A. et al. (1996) Nature Struc. Biol. 3, 803-811; Decanniere, K. et al. (1999) Structure 7, 361-370). However, the small size of these VHHs and their monomeric nature bring into question their capacity to bind haptens. Here, we have successfully raised llama antibodies against the hapten azo-dye Reactive Red (RR6) and determined the crystal structure of the complex between a dimer of this hapten and a VHH fragment. The surface of interaction between the VHH and the dimeric hapten is large, with an area of ca. 300 A(2); this correlates well with the low-dissociation constant of 22 nM measured for the monomer. The VHH fragment provides an efficient combining site to the RR6, using its three CDR loops. In particular, CDR1 provides a strong interaction to the hapten through two histidine residues bound to its copper atoms. VHH fragments might, therefore, prove to be valuable tools for selecting, removing, or capturing haptens. They are likely to play a role in biotechnology extending beyond protein recognition alone. |
==About this Structure== | ==About this Structure== | ||
| - | 1QD0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lama_glama Lama glama] with CU and RR6 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1QD0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lama_glama Lama glama] with <scene name='pdbligand=CU:'>CU</scene> and <scene name='pdbligand=RR6:'>RR6</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QD0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Brown, K.]] | [[Category: Brown, K.]] | ||
[[Category: Cambillau, C.]] | [[Category: Cambillau, C.]] | ||
| - | [[Category: Frenken, L | + | [[Category: Frenken, L G.J.]] |
[[Category: Hermans, P.]] | [[Category: Hermans, P.]] | ||
[[Category: Spinelli, S.]] | [[Category: Spinelli, S.]] | ||
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[[Category: immunoglobulin fragment]] | [[Category: immunoglobulin fragment]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:19 2008'' |
Revision as of 12:38, 21 February 2008
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CAMELID HEAVY CHAIN VARIABLE DOMAINS PROVIDE EFFICIENT COMBINING SITES TO HAPTENS
Overview
Camelids can produce antibodies devoid of light chains and CH1 domains (Hamers-Casterman, C. et al. (1993) Nature 363, 446-448). Camelid heavy-chain variable domains (VHH) have high affinities for protein antigens and the structures of two of these complexes have been determined (Desmyter, A. et al. (1996) Nature Struc. Biol. 3, 803-811; Decanniere, K. et al. (1999) Structure 7, 361-370). However, the small size of these VHHs and their monomeric nature bring into question their capacity to bind haptens. Here, we have successfully raised llama antibodies against the hapten azo-dye Reactive Red (RR6) and determined the crystal structure of the complex between a dimer of this hapten and a VHH fragment. The surface of interaction between the VHH and the dimeric hapten is large, with an area of ca. 300 A(2); this correlates well with the low-dissociation constant of 22 nM measured for the monomer. The VHH fragment provides an efficient combining site to the RR6, using its three CDR loops. In particular, CDR1 provides a strong interaction to the hapten through two histidine residues bound to its copper atoms. VHH fragments might, therefore, prove to be valuable tools for selecting, removing, or capturing haptens. They are likely to play a role in biotechnology extending beyond protein recognition alone.
About this Structure
1QD0 is a Single protein structure of sequence from Lama glama with and as ligands. Full crystallographic information is available from OCA.
Reference
Camelid heavy-chain variable domains provide efficient combining sites to haptens., Spinelli S, Frenken LG, Hermans P, Verrips T, Brown K, Tegoni M, Cambillau C, Biochemistry. 2000 Feb 15;39(6):1217-22. PMID:10684599
Page seeded by OCA on Thu Feb 21 14:38:19 2008
Categories: Lama glama | Single protein | Brown, K. | Cambillau, C. | Frenken, L G.J. | Hermans, P. | Spinelli, S. | Tegoni, M. | Verrips, T. | CU | RR6 | Azo-dye | Camelid vh | Immune system | Immunoglobulin fragment
