1i3u
From Proteopedia
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|PDB= 1i3u |SIZE=350|CAPTION= <scene name='initialview01'>1i3u</scene>, resolution 1.95Å | |PDB= 1i3u |SIZE=350|CAPTION= <scene name='initialview01'>1i3u</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CGN:5-OXO-PYRROLIDINE-2-CARBALDEHYDE'>CGN</scene>, <scene name='pdbligand=RR1:5-(4,6-DIAMINO-[1,3,5]TRIAZIN-2-YLAMINO)-4-HYDROXY-3-(2-SULFO-PHENYLAZO)-NAPHTHALENE-2,7-DISULFONIC+ACID'>RR1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1i3v|1I3V]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i3u OCA], [http://www.ebi.ac.uk/pdbsum/1i3u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i3u RCSB]</span> | ||
}} | }} | ||
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[[Category: Tegoni, M.]] | [[Category: Tegoni, M.]] | ||
[[Category: Vliet, C van.]] | [[Category: Vliet, C van.]] | ||
- | [[Category: RR1]] | ||
- | [[Category: SO4]] | ||
[[Category: antibody]] | [[Category: antibody]] | ||
[[Category: lama glama]] | [[Category: lama glama]] | ||
[[Category: vhh fragment]] | [[Category: vhh fragment]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:12 2008'' |
Revision as of 18:14, 30 March 2008
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, resolution 1.95Å | |||||||
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Ligands: | , , | ||||||
Related: | 1I3V
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
THREE-DIMENSIONAL STRUCTURE OF A LLAMA VHH DOMAIN COMPLEXED WITH THE DYE RR1
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
1I3U 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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